On the public citation graph

Multicopper Oxidases and Oxygenases

https://doi.org/10.1021/cr950046o
0 signed · 3969 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/9780470123164openalex-snapshot
Advances in Enzymology and Related Areas of Molecular Biology
inferredcites →https://doi.org/10.1002/j.1460-2075.1982.tb01313.xopenalex-snapshot
The structure of the paramagnetic oxygen intermediate in the cytochrome c oxidase reaction.
inferredcites →https://doi.org/10.1002/j.1537-2197.1941.tb07988.xopenalex-snapshot
RELATION OF VITAMIN C TO CELL SIZE IN THE GROWING REGION OF THE PRIMARY ROOT OF COWPEA SEEDLINGS
inferredcites →https://doi.org/10.1002/j.1537-2197.1961.tb11658.xopenalex-snapshot
DISTRIBUTION AND CELLULAR LOCALIZATION OF ASCORBIC ACID OXIDASE IN THE MAIZE ROOT TIP
inferredcites →https://doi.org/10.1002/macp.1978.021790105openalex-snapshot
Laccase‐catalyzed polymerization of urushiol in precisely confined Japanese lacquer system
inferredcites →https://doi.org/10.1002/pro.5560020411openalex-snapshot
Crystal structure of deoxygenated limulus polyphemus subunit II hemocyanin at 2.18 Å resolution: Clues for a mechanism for allosteric regulation
inferredcites →https://doi.org/10.1002/prot.340190405openalex-snapshot
Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences
inferredcites →https://doi.org/10.1006/abbi.1993.1487openalex-snapshot
The State of the Copper Sites in Human Ceruloplasmin
inferredcites →https://doi.org/10.1006/abbi.1995.1413openalex-snapshot
Detergent Solubilization of Membrane-Bound Methane Monooxygenase Requires Plastoquinol Analogs as Electron Donors
inferredcites →https://doi.org/10.1006/bbrc.1994.2350openalex-snapshot
Substrate Specificity of Ascorbate Oxidase: Unexpected Similarity to the Reduction Site of Dopamine β-Monooxygenase
inferredcites →https://doi.org/10.1006/bbrc.1994.2524openalex-snapshot
Sequence of the Gene, amoB, for the 43-kDa Polypeptide of Ammonia Monoxygenase of Nitrosomonas europaea
inferredcites →https://doi.org/10.1006/jmbi.1993.1215openalex-snapshot
X-ray Structures and Mechanistic Implications of Three Functional Derivatives of Ascorbate Oxidase from Zucchini
inferredcites →https://doi.org/10.1006/jmbi.1994.1335openalex-snapshot
Crystal Structure of a Free Radical Enzyme, Galactose Oxidase
inferredcites →https://doi.org/10.1007/978-94-011-0255-1_28openalex-snapshot
Purple Acid Phosphatases and Catechol Oxidase and their Model Compounds. Crystal Structure Studies of Purple Acid Phosphatase from Red Kidney Beans
inferredcites →https://doi.org/10.1007/978-94-011-0609-2openalex-snapshot
Active Oxygen in Biochemistry
inferredcites →https://doi.org/10.1007/978-94-011-6875-5openalex-snapshot
Bioinorganic Chemistry of Copper
inferredcites →https://doi.org/10.1007/978-94-011-6875-5_15openalex-snapshot
The Copper Ions in the Membrane-Associated Methane Monooxygenase
inferredcites →https://doi.org/10.1007/bf00124489openalex-snapshot
Trichloroethylene oxidation by the membrane-associated methane monooxygenase in type I, type II and type X methanotrophs
inferredcites →https://doi.org/10.1007/bf00195678openalex-snapshot
Extracellular laccases and peroxidases from sycamore maple (Acer pseudoplatanus) cell-suspension cultures
inferredcites →https://doi.org/10.1007/bf00227210openalex-snapshot
A reinvestigation on the quaternary structure of ascorbate oxidase from Cucurbita pepo medullosa
inferredcites →https://doi.org/10.1007/bf00230398openalex-snapshot
Sheep ceruloplasmin: isolation and characterization
inferredcites →https://doi.org/10.1007/bf00405880openalex-snapshot
Enzymatic synthesis of (+)- and (-)-bisdechlorogeodin with sulochrin oxidase from Penicillium frequentans and Oospora sulphurea-ochracea
inferredcites →https://doi.org/10.1007/bf00412178openalex-snapshot
Die Phenoloxydasen des Ascomyceten Podospora anserina
inferredcites →https://doi.org/10.1007/bf00425105openalex-snapshot
The importance of phenol oxidase activity in lignin degradation by the white-rot fungus Sporotrichum pulverulentum
inferredcites →https://doi.org/10.1007/bf01020827openalex-snapshot
Laccase fromPleurotus ostreatus
inferredcites →https://doi.org/10.1007/bf01785774openalex-snapshot
Multiple forms of soluble monophenol, dihydroxyphenylalanine: oxygen-oxidoreduetase (EC 1.14.1$.1) from potato tubers (Solanum tuberosum)
inferredcites →https://doi.org/10.1007/bf02208621openalex-snapshot
The identification and characterization of four laccases from the plant pathogenic fungus Rhizoctonia solani
inferredcites →https://doi.org/10.1007/bf02407305openalex-snapshot
Evolution of protein complexity: The blue copper-containing oxidases and related proteins
inferredcites →https://doi.org/10.1007/bf02425362openalex-snapshot
Multiple forms of soluble monophenol, dihydroxyphenylalanine: Oxygen-oxidoreductase (EC 1.14.18.1) from potato tubers (Solarium tuberosum)
inferredcites →https://doi.org/10.1007/bf02789129openalex-snapshot
The effect of albumin, ceruloplasmin, and other serum constitutents on Fe(II) oxidation
inferredcites →https://doi.org/10.1007/s007750050018openalex-snapshot
The X-ray structure of human serum ceruloplasmin at 3.1 Å: nature of the copper centres
inferredcites →https://doi.org/10.1016/0003-9861(62)90214-xopenalex-snapshot
The tritium rate effect in tyrosinase-catalyzed hydroxylation
inferredcites →https://doi.org/10.1016/0003-9861(65)90436-4openalex-snapshot
Ascorbic acid oxidase and ascorbic acid oxygenase of Myrothecium verrucaria
inferredcites →https://doi.org/10.1016/0003-9861(68)90531-6openalex-snapshot
Kinetic studies of ferrous ion oxidation with crystalline human ferroxidase
inferredcites →https://doi.org/10.1016/0003-9861(69)90067-8openalex-snapshot
Enzymatic synthesis of actinocinyl peptides
inferredcites →https://doi.org/10.1016/0003-9861(81)90429-xopenalex-snapshot
Phenoxazinone synthase from Streptomyces antibioticus: Purification of the large and small enzyme forms
inferredcites →https://doi.org/10.1016/0003-9861(85)90374-1openalex-snapshot
Characterization of cucumber ascorbate oxidase and its reaction with hexacyanoferrate (II)
inferredcites →https://doi.org/10.1016/0003-9861(85)90568-5openalex-snapshot
Purification and partial characterization of ceruloplasmin from chicken serum
inferredcites →https://doi.org/10.1016/0003-9861(88)90172-5openalex-snapshot
Degradation mechanisms of phenolic β-1 lignin substructure model compounds by laccase of Coriolus versicolor
inferredcites →https://doi.org/10.1016/0003-9861(88)90419-5openalex-snapshot
Purification and partial characterization of goose ceruloplasmin
inferredcites →https://doi.org/10.1016/0003-9861(90)90083-bopenalex-snapshot
Purification and partial characterization of ceruloplasmin receptors from rat liver endothelium
inferredcites →https://doi.org/10.1016/0003-9861(90)90455-8openalex-snapshot
Unusual stability properties of a reptilian ceruloplasmin
inferredcites →https://doi.org/10.1016/0005-2728(69)90219-9openalex-snapshot
Studies of the heme components of cytochrome c oxidase by EPR spectroscopy
inferredcites →https://doi.org/10.1016/0005-2728(70)90059-9openalex-snapshot
Purification and properties of laccase and stellacyanin from Rhus vernicifera
inferredcites →https://doi.org/10.1016/0005-2728(72)90045-xopenalex-snapshot
Oxidation-reduction potentials of the electron acceptors in laccases and stellacyanin
inferredcites →https://doi.org/10.1016/0005-2744(76)90112-1openalex-snapshot
Kinetic studies of Rhus vernicifera laccase
inferredcites →https://doi.org/10.1016/0005-2744(78)90166-3openalex-snapshot
The effect of pH on the oxygen intermediate and the dioxygen reducing site in blue oxidases
inferredcites →https://doi.org/10.1016/0005-2744(78)90292-9openalex-snapshot
Steady-state kinetics of laccase from Rhus vernicifera
inferredcites →https://doi.org/10.1016/0005-2744(79)90282-1openalex-snapshot
The mechanism of electron transfer in laccase-catalysed reactions
inferredcites →https://doi.org/10.1016/0005-2795(70)90168-6openalex-snapshot
Evidence of a specific copper(II) in human ceruloplasmin as a binding site for inhibitory anions
inferredcites →https://doi.org/10.1016/0005-2795(72)90182-1openalex-snapshot
Visible and near-infrared circular dichroism of some blue copper proteins
inferredcites →https://doi.org/10.1016/0005-2795(73)90006-8openalex-snapshot
Anion-binding and the state of copper in caeruloplasmin
inferredcites →https://doi.org/10.1016/0005-2795(73)90112-8openalex-snapshot
The stoichiometry of the paramagnetic copper and the oxidation-reduction potentials of type I copper in human ceruloplasmin
inferredcites →https://doi.org/10.1016/0005-2795(73)90267-5openalex-snapshot
The intracellular distribution of the radiocopper derived from ceruloplasmin and from albumin
inferredcites →https://doi.org/10.1016/0005-2795(73)90268-7openalex-snapshot
The association of the copper derived from ceruloplasmin with cytocuprein
inferredcites →https://doi.org/10.1016/0005-2795(75)90090-2openalex-snapshot
EPR studies on the anaerobic reduction of fungal laccase
inferredcites →https://doi.org/10.1016/0005-2795(75)90292-5openalex-snapshot
The phenoloxidases of the ascomycete Podospora anserina XI. The state of copper of laccases I, II and III
inferredcites →https://doi.org/10.1016/0005-2795(76)90080-5openalex-snapshot
Ceruloplasmin-anion interaction a circular dichroism spectroscopic study
inferredcites →https://doi.org/10.1016/0005-2795(76)90264-6openalex-snapshot
Absorption and circular dichroism spectra of different forms of mushroom tyrosinase
inferredcites →https://doi.org/10.1016/0005-2795(78)90470-1openalex-snapshot
The state of copper in Neurospora laccase
inferredcites →https://doi.org/10.1016/0006-291x(75)90172-2openalex-snapshot
Evidence for ceruloplasmin as a copper transport protein
inferredcites →https://doi.org/10.1016/0006-291x(76)90734-8openalex-snapshot
Oxidative titrations of Rhusvernicifera laccase and its specific interaction with hydrogen peroxide
inferredcites →https://doi.org/10.1016/0006-291x(76)91030-5openalex-snapshot
A 17O-effect on the EPR spectrum of the intermediate in the dioxygen-laccase reaction
inferredcites →https://doi.org/10.1016/0006-291x(76)91077-9openalex-snapshot
Quaternary structure of mushroom tyrosinase
inferredcites →https://doi.org/10.1016/0006-291x(78)90170-5openalex-snapshot
Chemical and spectroscopic conformation of an exogenous ligand bridge in half met hemocyanin
inferredcites →https://doi.org/10.1016/0006-291x(78)91655-8openalex-snapshot
Spectroscopic studies of ligand perturbation effects on the half oxidized active site of busycon canaliculatum hemocyanin
inferredcites →https://doi.org/10.1016/0006-291x(79)91759-5openalex-snapshot
Reactions and interconversion of met and dimer hemocyanin
inferredcites →https://doi.org/10.1016/0006-291x(79)92114-4openalex-snapshot
Ligand displacement reactions of oxyhemocyanin: Comparison of reactivities of arthropods and molluscs
inferredcites →https://doi.org/10.1016/0006-3002(63)90304-4openalex-snapshot
Purification and some properties of laccase from Polyporus versicolor
inferredcites →https://doi.org/10.1016/0006-3002(63)91867-5openalex-snapshot
Bacterial ascorbic acid oxidase
inferredcites →https://doi.org/10.1016/0009-2797(85)90043-2openalex-snapshot
Inhibition of the Fenton reaction by the protein caeruloplasmin and other copper complexes. Assessment of ferroxidase and radical scavenging activities
inferredcites →https://doi.org/10.1016/0014-5793(68)80016-xopenalex-snapshot
The requirement of the “non‐blue” copper (II) for the activity of fungal laccase
inferredcites →https://doi.org/10.1016/0014-5793(72)80025-5openalex-snapshot
Monomer and magnetic dipole‐coupled Cu2+ EPR signals in nitrosylhemocyanin
inferredcites →https://doi.org/10.1016/0014-5793(73)80768-9openalex-snapshot
An intermediate in the reaction of reduced laccase with oxygen
inferredcites →https://doi.org/10.1016/0014-5793(74)80736-2openalex-snapshot
The stoichiometry of the three different types of copper in ascorbate oxidase from green zucchini squash
inferredcites →https://doi.org/10.1016/0014-5793(76)80675-8openalex-snapshot
Neurospora tyrosinase: Molecular weight, copper content and spectral properties
inferredcites →https://doi.org/10.1016/0014-5793(76)80732-6openalex-snapshot
Selective removal of type 2 copper from Rhus vernicifera laccase
inferredcites →https://doi.org/10.1016/0014-5793(76)81016-2openalex-snapshot
A paramagnetic intermediate in the reduction of oxygen by reduced laccase
inferredcites →https://doi.org/10.1016/0014-5793(77)80967-8openalex-snapshot
Type 2 copper(II) as a component of the dioxygen reducing site in laccase: Evidence from EPR experiments with 17 O
inferredcites →https://doi.org/10.1016/0014-5793(80)80195-5openalex-snapshot
Oxygen free‐radicals and lipid peroxidation: inhibition by the protein caeruloplasmin
inferredcites →https://doi.org/10.1016/0014-5793(82)80788-6openalex-snapshot
The role of superoxide and hydroxyl radicals in phospholipid peroxidation catalysed by iron salts
inferredcites →https://doi.org/10.1016/0014-5793(83)80432-3openalex-snapshot
Ceruloplasmin and the reactions forming differic transferrin
inferredcites →https://doi.org/10.1016/0014-5793(83)81111-9openalex-snapshot
Antioxidant properties of caeruloplasmin towards iron‐ and copper‐dependent oxygen radical formation
inferredcites →https://doi.org/10.1016/0014-5793(90)80273-lopenalex-snapshot
A novel combination of prosthetic groups in a fungal laccase; PQQ and two copper atoms
inferredcites →https://doi.org/10.1016/0014-5793(90)80298-wopenalex-snapshot
Oxidation of non‐phenolic substrates
inferredcites →https://doi.org/10.1016/0014-5793(91)81331-2openalex-snapshot
A model of the copper centres of nitrous oxide reductase (Pseudomonas stutzeri)
inferredcites →https://doi.org/10.1016/0016-0032(66)90569-2openalex-snapshot
Ligand substitution processes
inferredcites →https://doi.org/10.1016/0020-1790(81)90036-6openalex-snapshot
Phenoloxidases in larval cuticle of the blowfly, Calliphora vicina
inferredcites →https://doi.org/10.1016/0020-1790(89)90095-4openalex-snapshot
A trypsin-solubilized laccase from pharate pupal integument of the tobacco hornworm, Manduca sexta
inferredcites →https://doi.org/10.1016/0020-711x(94)90038-8openalex-snapshot
Bioinorganic chemistry of copper
inferredcites →https://doi.org/10.1016/0022-2836(89)90276-3openalex-snapshot
Crystal structure of hexameric haemocyanin from Panulirus interruptus refined at 3.2 Å resolution
inferredcites →https://doi.org/10.1016/0022-2836(89)90498-1openalex-snapshot
X-ray crystal structure of the blue oxidase ascorbate oxidase from Zucchini
inferredcites →https://doi.org/10.1016/0022-2836(92)90583-6openalex-snapshot
Refined crystal structure of ascorbate oxidase at 1.9 Å resolution
inferredcites →https://doi.org/10.1016/0031-9422(75)80349-9openalex-snapshot
Molecular weight and amino acid composition of purified spinach beet phenolase
inferredcites →https://doi.org/10.1016/0031-9422(79)80057-6openalex-snapshot
Polyphenol oxidases in plants
inferredcites →https://doi.org/10.1016/0031-9422(92)83427-zopenalex-snapshot
Cell wall-bound coniferyl alcohol oxidase associated with lignification in conifers
inferredcites →https://doi.org/10.1016/0040-4020(89)80033-xopenalex-snapshot
Synthetic models for binuclear copper proteins
inferredcites →https://doi.org/10.1016/0040-4039(93)85091-aopenalex-snapshot
Structural Elucidation of a Putative Conidial Pigment Intermediate in Aspergillus parasiticus
inferredcites →https://doi.org/10.1016/0076-6879(71)17251-5openalex-snapshot
[79] Tyrosinase (mushroom)
inferredcites →https://doi.org/10.1016/0092-8674(94)90346-8openalex-snapshot
The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake
inferredcites →https://doi.org/10.1016/0141-0229(91)90005-uopenalex-snapshot
Lignin degradation by Rigidoporus lignosus involves synergistic action of two oxidizing enzymes: Mn peroxidase and laccase
inferredcites →https://doi.org/10.1016/0162-0134(85)85008-xopenalex-snapshot
A room temperature electron paramagnetic resonance study of native and fluoride-reacted vietnamese and japanese lacquer-tree laccases: differences from liquid-nitrogen spectra
inferredcites →https://doi.org/10.1016/0162-0134(86)80043-5openalex-snapshot
Different origins of metal binding sites in binuclear copper proteins, tyrosinase and hemocyanin
inferredcites →https://doi.org/10.1016/0162-0134(94)00056-gopenalex-snapshot
The role of copper in the pMMO of Methylococcus capsulatus Bath: A structural vs. catalytic function
inferredcites →https://doi.org/10.1016/0167-4838(84)90257-7openalex-snapshot
Extended X-ray absorption fine structure study of the coupled binuclear copper active site of tyrosinase from Neurospora crassa
inferredcites →https://doi.org/10.1016/0167-4838(95)00104-3openalex-snapshot
Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases
inferredcites →https://doi.org/10.1016/0167-7799(83)90026-4openalex-snapshot
The biochemistry of methylotrophs
inferredcites →https://doi.org/10.1016/0300-9629(92)90261-nopenalex-snapshot
Response of protein turnover in the brown tiger prawn Penaeus esculentus to variation in dietary protein content
inferredcites →https://doi.org/10.1016/0301-4622(94)00110-6openalex-snapshot
Effect of subzero incubation on fluoride binding by laccase
inferredcites →https://doi.org/10.1016/0301-4622(94)00156-eopenalex-snapshot
Rapid electron injection into multisite metalloproteins: intramolecular electron transfer in cytochrome oxidase
inferredcites →https://doi.org/10.1016/0304-4165(68)90105-0openalex-snapshot
Two forms of copper (II) in fungal laccase
inferredcites →https://doi.org/10.1016/0304-4165(68)90199-2openalex-snapshot
Degradation of the lignin model compount springgylglycol-β-guaiacyl ether by Polyporus versicolor and Stereum frustulatum
inferredcites →https://doi.org/10.1016/0304-4165(82)90389-0openalex-snapshot
Kinetic study of the pathway of melanizationn between l-dopa and dopachrome
inferredcites →https://doi.org/10.1016/0304-4165(87)90003-1openalex-snapshot
A kinetic study of the melanization pathway between L-tyrosine and dopachrome
inferredcites →https://doi.org/10.1016/0304-4165(93)90129-vopenalex-snapshot
Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins
inferredcites →https://doi.org/10.1016/0304-4173(85)90014-xopenalex-snapshot
Electron transfers in chemistry and biology
inferredcites →https://doi.org/10.1016/0378-1097(92)90135-bopenalex-snapshot
Extracellular enzyme localization during interspecific fungal interactions
inferredcites →https://doi.org/10.1016/0885-5765(91)90010-fopenalex-snapshot
Evidence for oxidative detoxication of pterostilbene and resveratrol by a laccase-like stilbene oxidase produced by Botrytis cinerea
inferredcites →https://doi.org/10.1016/b978-0-12-347880-1.50011-8openalex-snapshot
Biosynthesis of Lignin
inferredcites →https://doi.org/10.1016/s0005-2728(05)80204-xopenalex-snapshot
Characterisation of ‘fast’ and ‘slow’ forms of bovine heart cytochrome-c oxidase
inferredcites →https://doi.org/10.1016/s0005-2728(89)80087-8openalex-snapshot
The effect of pH and temperature on the reaction of fully reduced and mixed-valence cytochrome c oxidase with dioxygen
inferredcites →https://doi.org/10.1016/s0006-291x(72)80223-7openalex-snapshot
Reversible oxygenation of tyrosinase
inferredcites →https://doi.org/10.1016/s0006-291x(75)80066-0openalex-snapshot
Ceruloplasmin-anion interaction a resonance Raman spectroscopic study
inferredcites →https://doi.org/10.1016/s0006-291x(77)80208-8openalex-snapshot
The protective action of superoxide dismutase on metal-ion catalysed peroxidation of phospholipids
inferredcites →https://doi.org/10.1016/s0006-291x(84)80348-4openalex-snapshot
Ceruloplasmin receptors of erythrocytes
inferredcites →https://doi.org/10.1016/s0006-291x(86)80064-xopenalex-snapshot
Binding and uptake of copper from ceruloplasmin
inferredcites →https://doi.org/10.1016/s0010-8545(00)80255-6openalex-snapshot
The determination of structural properties of dimeric transition metal ion complexes from epr spectra
inferredcites →https://doi.org/10.1016/s0020-1693(00)81205-0openalex-snapshot
Dioxygen-copper reactivity: intermediacy of a peroxo-dicopper(II) (dioxygen-copper) complex in the hydroxylation reaction of a model mono-oxygenase system
inferredcites →https://doi.org/10.1016/s0020-1693(00)81784-3openalex-snapshot
Peroxide and redox titrations of type 2 copper depleted laccase
inferredcites →https://doi.org/10.1016/s0020-1693(00)85677-7openalex-snapshot
Distinction of the two type I coppers in bovine ceruloplasmin
inferredcites →https://doi.org/10.1016/s0021-9258(17)34362-4openalex-snapshot
Electronic state of heme in cytochrome oxidase III. The magnetic susceptibility of beef heart cytochrome oxidase and some of its derivatives from 7-200 K. Direct evidence for an antiferromagnetically coupled Fe (III)/Cu (II) pair.
inferredcites →https://doi.org/10.1016/s0021-9258(17)36565-1openalex-snapshot
The nature of the copper ions in the membranes containing the particulate methane monooxygenase from Methylococcus capsulatus (Bath).
inferredcites →https://doi.org/10.1016/s0021-9258(17)46699-3openalex-snapshot
Molecular cloning of the gene for bilirubin oxidase from Myrothecium verrucaria and its expression in yeast.
inferredcites →https://doi.org/10.1016/s0021-9258(18)35647-3openalex-snapshot
Protein control of iron-sulfur cluster redox potentials.
inferredcites →https://doi.org/10.1016/s0021-9258(18)43890-2openalex-snapshot
Selective resonance Raman observation of the “607 nm” form generated in the reaction of oxidized cytochrome c oxidase with hydrogen peroxide.
inferredcites →https://doi.org/10.1016/s0021-9258(18)45979-0openalex-snapshot
14C2H2- and 14CO2-labeling studies of the de novo synthesis of polypeptides by Nitrosomonas europaea during recovery from acetylene and light inactivation of ammonia monooxygenase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)52231-6openalex-snapshot
The reaction of the electrostatic cytochrome c-cytochrome oxidase complex with oxygen
inferredcites →https://doi.org/10.1016/s0021-9258(18)60387-4openalex-snapshot
Biosynthesis of the Actinomycin Chromophore; Enzymatic Conversion of 4-Methyl-3-hydroxyanthranilic Acid to Actinocin
inferredcites →https://doi.org/10.1016/s0021-9258(18)62943-6openalex-snapshot
Substrate Activation and the Kinetics of Ferroxidase
inferredcites →https://doi.org/10.1016/s0021-9258(18)62944-8openalex-snapshot
The Inhibition of Ferroxidase by Trivalent and Other Metal Ions
inferredcites →https://doi.org/10.1016/s0021-9258(18)63623-3openalex-snapshot
Mobilization of Liver Iron by Ferroxidase (Ceruloplasmin)
inferredcites →https://doi.org/10.1016/s0021-9258(18)68666-1openalex-snapshot
Chicken ceruloplasmin. Evidence in support of a trinuclear cluster involving type 2 and 3 copper centers.
inferredcites →https://doi.org/10.1016/s0021-9258(18)68751-4openalex-snapshot
The active site of galactose oxidase.
inferredcites →https://doi.org/10.1016/s0021-9258(18)71485-3openalex-snapshot
Isolation and Characterization of the Tyrosinase Gene from Neurospora crassa
inferredcites →https://doi.org/10.1016/s0021-9258(18)83138-6openalex-snapshot
Electron transfer process in cytochrome oxidase after pulse radiolysis
inferredcites →https://doi.org/10.1016/s0021-9258(18)83399-3openalex-snapshot
An X-ray Crystallographic Study of Ceruloplasmin
inferredcites →https://doi.org/10.1016/s0021-9258(18)93295-3openalex-snapshot
Ceruloplasmin-Anion Interactions
inferredcites →https://doi.org/10.1016/s0021-9258(18)96527-0openalex-snapshot
The Possible Significance of the Ferrous Oxidase Activity of Ceruloplasmin in Normal Human Serum
inferredcites →https://doi.org/10.1016/s0021-9258(18)96973-5openalex-snapshot
The Tyrosine Hydroxylase Activity of Mammalian Tyrosinase
inferredcites →https://doi.org/10.1016/s0021-9258(18)97320-5openalex-snapshot
A Comparison of the Enzymic Activities of Pig Ceruloplasmin and Rhus vernicifera Laccase
inferredcites →https://doi.org/10.1016/s0021-9258(18)99620-1openalex-snapshot
Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase
inferredcites →https://doi.org/10.1016/s0021-9258(18)99669-9openalex-snapshot
Kinetic Studies of Ferrous Ion Oxidation with Crystalline Human Ferroxidase (Ceruloplasmin)
inferredcites →https://doi.org/10.1016/s0021-9258(19)35436-5openalex-snapshot
Characterization of two allelic forms of Neurospora crassa laccase. Amino- and carboxyl-terminal processing of a precursor.
inferredcites →https://doi.org/10.1016/s0021-9258(19)36753-5openalex-snapshot
Regulation of iron uptake in Saccharomyces cerevisiae. The ferrireductase and Fe(II) transporter are regulated independently.
inferredcites →https://doi.org/10.1016/s0021-9258(19)38663-6openalex-snapshot
Age-related changes in human ceruloplasmin. Evidence for oxidative modifications
inferredcites →https://doi.org/10.1016/s0021-9258(19)40634-0openalex-snapshot
Functional intermediates in the reaction of membrane-bound cytochrome oxidase with oxygen.
inferredcites →https://doi.org/10.1016/s0021-9258(19)43035-4openalex-snapshot
Oxytyrosinase
inferredcites →https://doi.org/10.1016/s0021-9258(19)43565-5openalex-snapshot
Reactivity of Oxytyrosinase toward Substrates
inferredcites →https://doi.org/10.1016/s0021-9258(19)50597-xopenalex-snapshot
Analysis of a kinetic model for melanin biosynthesis pathway.
inferredcites →https://doi.org/10.1016/s0021-9258(19)67974-3openalex-snapshot
Studies on the State of Copper in Native and Modified Human Ceruloplasmin
inferredcites →https://doi.org/10.1016/s0021-9258(19)69961-8openalex-snapshot
Structural studies of asparagine-linked sugar chains of human ceruloplasmin. Structural characteristics of the triantennary complex type sugar chains of human plasma glycoproteins.
inferredcites →https://doi.org/10.1016/s0021-9258(19)75655-5openalex-snapshot
Evidence for a ferryl Fea3 in oxygenated cytochrome c oxidase.
inferredcites →https://doi.org/10.1016/s0021-9258(19)77137-3openalex-snapshot
Physicochemical and Kinetic Properties of Mushroom Tyrosinase
inferredcites →https://doi.org/10.1016/s0021-9258(20)65157-2openalex-snapshot
Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether.
inferredcites →https://doi.org/10.1016/s0022-2836(67)80005-6openalex-snapshot
Low temperature magnetic susceptibility of ceruloplasmin
inferredcites →https://doi.org/10.1016/s0031-9422(00)80367-2openalex-snapshot
Isolation and characterization of the polyphenoloxidase from senescent leaves of black poplar
inferredcites →https://doi.org/10.1016/s0031-9422(00)80734-7openalex-snapshot
The effect of fungal laccase on fractionated lignosulphonates (peritan Na)
inferredcites →https://doi.org/10.1016/s0031-9422(00)84503-3openalex-snapshot
Cooperation between fungal laccase and glucose oxidase in the degradation of lignin derivatives
inferredcites →https://doi.org/10.1016/s0031-9422(00)85210-3openalex-snapshot
A critical study of the intracellular distribution of ascorbate oxidase and a comparison of the kinetics of the soluble and cell-wall enzyme
inferredcites →https://doi.org/10.1016/s0031-9422(00)90338-8openalex-snapshot
Oxidation of coniferyl alcohol to lignin-like products by tobacco xylem cell walls
inferredcites →https://doi.org/10.1016/s0162-0134(00)80133-6openalex-snapshot
An epr signal from the half-reduced type 3 copper pair in Rhus vernicifera laccase
inferredcites →https://doi.org/10.1016/s0162-0134(00)80177-4openalex-snapshot
Spectroscopic and catalytic properties of rhus vernicifera laccase depleted in type 2 copper
inferredcites →https://doi.org/10.1016/s0953-7562(09)80598-4openalex-snapshot
The Pgr1 mutant of Cochliobolus heterostrophus lacks a p-diphenol oxidase involved in naphthalenediol melanin synthesis
inferredcites →https://doi.org/10.1021/ar00030a006openalex-snapshot
Vectorial chemistry in bioenergetics: cytochrome c oxidase as a redox-linked proton pump
inferredcites →https://doi.org/10.1021/bi00037a011openalex-snapshot
NIH shift in the hydroxylation of aromatic compounds by the ammonia-oxidizing bacterium Nitrosomonas europaea. Evidence against an arene oxide intermediate
inferredcites →https://doi.org/10.1021/bi00042a011openalex-snapshot
The Interaction of Cytochrome Oxidase with Hydrogen Peroxide: The Relationship of Compounds P and F
inferredcites →https://doi.org/10.1021/bi00069a018openalex-snapshot
Stoichiometry and spectroscopic identity of copper centers in phenoxazinone synthase: A new addition to the blue copper oxidase family
inferredcites →https://doi.org/10.1021/bi00082a003openalex-snapshot
Magnetization of fast and slow oxidized cytochrome c oxidase
inferredcites →https://doi.org/10.1021/bi00176a042openalex-snapshot
Oxygen Binding and Activation: Early Steps in the Reaction of Oxygen with Cytochrome c Oxidase
inferredcites →https://doi.org/10.1021/bi00232a037openalex-snapshot
Direct measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme ascorbate oxidase and its type II copper-depleted and cyanide-inhibited forms
inferredcites →https://doi.org/10.1021/bi00297a014openalex-snapshot
Specific receptor for ceruloplasmin in membrane fragments from aortic and heart tissues
inferredcites →https://doi.org/10.1021/bi00304a027openalex-snapshot
Effects of a single reduction-reoxidation cycle on the kinetics of copper reductions in Rhus laccase
inferredcites →https://doi.org/10.1021/bi00343a003openalex-snapshot
Primary structure of tyrosinase from Streptomyces glaucescens
inferredcites →https://doi.org/10.1021/bi00415a032openalex-snapshot
Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase
inferredcites →https://doi.org/10.1021/bi00441a026openalex-snapshot
Phenoxazinone synthase: mechanism for the formation of the phenoxazinone chromophore of actinomycin
inferredcites →https://doi.org/10.1021/bi00443a030openalex-snapshot
Electron transfer between cytochrome a and copper A in cytochrome c oxidase: a perturbed equilibrium study
inferredcites →https://doi.org/10.1021/bi00489a014openalex-snapshot
Temperature and anation studies of the type 2 site in Rhus vernicifera laccase
inferredcites →https://doi.org/10.1021/bi00524a017openalex-snapshot
Histidine at the active site of Neurospora tyrosinase
inferredcites →https://doi.org/10.1021/bi00661a003openalex-snapshot
Reinvestigation of some physicochemical and chemical properties of human ceruloplasmin (ferroxidase)
inferredcites →https://doi.org/10.1021/bi00797a013openalex-snapshot
Binding of transition metal ions by ceruloplasmin (ferroxidase)
inferredcites →https://doi.org/10.1021/bi9511705openalex-snapshot
Microcirculating System for Simultaneous Determination of Raman and Absorption Spectra of Enzymatic Reaction Intermediates and Its Application to the Reaction of Cytochrome c Oxidase with Hydrogen Peroxide
inferredcites →https://doi.org/10.1021/bi952096topenalex-snapshot
Resonance Raman/Absorption Characterization of the Oxo Intermediates of Cytochrome c Oxidase Generated in Its Reaction with Hydrogen Peroxide: pH and H2O2 Concentration Dependence
inferredcites →https://doi.org/10.1021/bi952971aopenalex-snapshot
Oxidation of Phenols, Anilines, and Benzenethiols by Fungal Laccases: Correlation between Activity and Redox Potentials as Well as Halide Inhibition
inferredcites →https://doi.org/10.1021/bk-1995-0600openalex-snapshot
Enzymatic Browning and Its Prevention
inferredcites →https://doi.org/10.1021/cr00012a003openalex-snapshot
Electronic structures of active sites in copper proteins: contributions to reactivity
inferredcites →https://doi.org/10.1021/cr00027a010openalex-snapshot
Copper-Dioxygen Complexes. Inorganic and Bioinorganic Perspectives
inferredcites →https://doi.org/10.1021/cr00027a013openalex-snapshot
Spectroscopy of Binuclear Dioxygen Complexes
inferredcites →https://doi.org/10.1021/cr00105a008openalex-snapshot
Cytochrome c oxidase as a redox-linked proton pump
inferredcites →https://doi.org/10.1021/cr9500390openalex-snapshot
Structural and Functional Aspects of Metal Sites in Biology
inferredcites →https://doi.org/10.1021/cr950045wopenalex-snapshot
Protein Control of Redox Potentials of Iron−Sulfur Proteins
showing the first 200 of 386

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4102755openalex-extracted
Kinetic and Thermodynamic Analysis of Cu2+-Dependent Reductive Inactivation in Direct Electron Transfer-Type Bioelectrocatalysis by Copper Efflux Oxidase
inferred← citeshttps://doi.org/10.2139/ssrn.4350174openalex-extracted
Complete Oxidative Degradation of Diclofenac by Coupling Free Radicals and Oxygenases of a Micro-/Nanostructured Biogenic Mn Oxide Composite from Engineered Pseudomonas Sp. Mb04r-2
inferred← citeshttps://doi.org/10.5281/zenodo.10722openalex-extracted
Orbital Analysis Of Oxo And Peroxo Dicopper Complexes Via Quantum Chemical Workflows In Mosgrid
inferred← citeshttps://doi.org/10.1002/(sici)1097-458x(199908)37:8<538::aid-mrc498>3.0.co;2-0openalex-snapshot
An unusual temperature dependence of the EPR parameters of copper(II) and oxovanadium(IV) bis(acetylacetonate) complexes
inferred← citeshttps://doi.org/10.1002/(sici)1099-1409(199801/02)2:1<39::aid-jpp49>3.0.co;2-#openalex-snapshot
A poly(pyrrole‐copper(II) deuteroporphyrin) modified electrode
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19990115)111:1/2<180::aid-ange180>3.0.co;2-zopenalex-snapshot
Reaktivität von Peroxo- und Di-μ-oxo-dikupferkomplexen gegenüber Brenzcatechinen
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(19990419)111:8<1210::aid-ange1210>3.0.co;2-uopenalex-snapshot
Ist der Bis(μ-oxo)dikupfer-Kern fähig, ein Aren zu hydroxylieren?
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(20000117)112:2<409::aid-ange409>3.0.co;2-jopenalex-snapshot
Aliphatische Hydroxylierung mit einem Bis(μ-oxo)dikupfer(III)-Komplex
inferred← citeshttps://doi.org/10.1002/(sici)1521-3757(20000502)112:9<1656::aid-ange1656>3.0.co;2-bopenalex-snapshot
Wie funktioniert die Tyrosinase? Neue Einblicke aus Modellchemie und Strukturbiologie
inferred← citeshttps://doi.org/10.1002/0470028637.met196openalex-snapshot
Catechol Oxidase
inferred← citeshttps://doi.org/10.1002/0470028637.met199openalex-snapshot
Laccase
inferred← citeshttps://doi.org/10.1002/0470028637.met232openalex-snapshot
Particulate Methane Monooxygenase
inferred← citeshttps://doi.org/10.1002/0470028637.met254openalex-snapshot
Human Factor VIII
inferred← citeshttps://doi.org/10.1002/0470028637.met265openalex-snapshot
Structure, Spectroscopy, and Function of Tyrosinase; Comparison with Hemocyanin and Catechol Oxidase
inferred← citeshttps://doi.org/10.1002/0470862106.ia051openalex-snapshot
Copper: Hemocyanin/Tyrosinase ModelsBased in part on the article Copper: Hemocyanin/Tyrosinase Models by Nobumasa Kitajima which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/0470862106.ia054openalex-snapshot
Copper Proteins with Dinuclear Active SitesBased in part on the article Copper Proteins with Dinuclear Active Sites by Konrad Lerch which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/0470862106.ia055openalex-snapshot
Copper Proteins: Oxidases
inferred← citeshttps://doi.org/10.1002/0470862106.ia056openalex-snapshot
Copper Proteins with Type 1 SitesBased in part on the article Copper Proteins with Type 1 Sites by Edward N. Baker which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/0470862106.ia606openalex-snapshot
Quantum Mechanical/Molecular Mechanical ( QM / MM ) Methods and Applictions in Bioinorganic Chemistry
inferred← citeshttps://doi.org/10.1002/0471227617.eoc064.pub2openalex-snapshot
Copper Enzymes/Models
inferred← citeshttps://doi.org/10.1002/0471227617.eoc185openalex-snapshot
Selective Oxidation – Biological
inferred← citeshttps://doi.org/10.1002/1099-0682(200203)2002:4<987::aid-ejic987>3.0.co;2-ropenalex-snapshot
A New CuI Complex that Mimics the Cresolase Reaction of Tyrosinase and the Crystal Structure of its Oxygenated CuII Complex
inferred← citeshttps://doi.org/10.1002/1099-0682(200208)2002:8<2007::aid-ejic2007>3.0.co;2-zopenalex-snapshot
Supramolecular Assembly with Calix[6]arene and Copper Ions − Formation of a Novel Tetranuclear Core Exhibiting Unusual Redox Properties and Catecholase Activity
inferred← citeshttps://doi.org/10.1002/1099-0682(20021)2002:1<111::aid-ejic111>3.0.co;2-7openalex-snapshot
Syntheses and Characterization of Copper(II) Complexes of the New LigandsN-[(2-Pyridyl)methyl]-2,2′-dipyridylamine andN-[Bis(2-pyridyl)methyl]-2-pyridylamine
inferred← citeshttps://doi.org/10.1002/1099-0682(200211)2002:11<2857::aid-ejic2857>3.0.co;2-#openalex-snapshot
Dioxygen Activation Using Schiff Base Macrocyclic Dinuclear Copper( I ) Complexes: Structurally Characterized Dioxygen Reaction Products
inferred← citeshttps://doi.org/10.1002/1521-3757(20000616)112:12<2199::aid-ange2199>3.0.co;2-qopenalex-snapshot
μ4-Peroxo- versus Bis(μ2-hydroxo)-Einheiten in strukturell analogen Tetrakupfer(II)-Komplexen
inferred← citeshttps://doi.org/10.1002/1521-3757(20000616)112:12<2222::aid-ange2222>3.0.co;2-2openalex-snapshot
Structure of Homoleptic CuI(CO)3 Cations in CuI-Exchanged ZSM-5 Zeolite: An X-ray Absorption Study
inferred← citeshttps://doi.org/10.1002/1521-3757(20010105)113:1<76::aid-ange76>3.0.co;2-fopenalex-snapshot
Dendritisch eingeschlossene aktive Zentren: Anwendung des Isolationsprinzips der Natur in der Biomimetik und den Materialwissenschaften
inferred← citeshttps://doi.org/10.1002/1521-3757(20010119)113:2<358::aid-ange358>3.0.co;2-3openalex-snapshot
Chemisch modifizierte Aminosäuren in O2-bindenden oder -aktivierenden Kupferproteinen
inferred← citeshttps://doi.org/10.1002/1521-3757(20010417)113:8<1532::aid-ange1532>3.0.co;2-0openalex-snapshot
A Short Copper-Copper Distance in a (μ-1,2-Peroxo)dicopper(II) Complex Having a 1,8-Naphthyridine Unit as an Additional Bridge
inferred← citeshttps://doi.org/10.1002/1521-3757(20010803)113:15<2860::aid-ange2860>3.0.co;2-2openalex-snapshot
Aktivierung von Disauerstoff und Hydroxylierung von Methan durch lösliche Methan-Monooxygenase: eine Geschichte von zwei Eisenatomen und drei Proteinen
inferred← citeshttps://doi.org/10.1002/1521-3757(20011217)113:24<4702::aid-ange4702>3.0.co;2-6openalex-snapshot
Kupferproteine: Koordination und Aktivierung von Sauerstoff und seine Reduktion zu Wasser
inferred← citeshttps://doi.org/10.1002/1521-3757(20020402)114:7<1160::aid-ange1160>3.0.co;2-0openalex-snapshot
Biokatalytisch relevante rautenförmige Bis(μ-oxo)dimetall-Kerne in Kupfer- und Eisenkomplexen
inferred← citeshttps://doi.org/10.1002/1521-3765(20020104)8:1<247::aid-chem247>3.0.co;2-popenalex-snapshot
Tuning the Activity of Catechol Oxidase Model Complexes by Geometric Changes of the Dicopper Core
inferred← citeshttps://doi.org/10.1002/1521-3773(20000616)39:12<2138::aid-anie2138>3.0.co;2-9openalex-snapshot
Structure of Homoleptic CuI(CO)3 Cations in CuI-Exchanged ZSM-5 Zeolite: An X-ray Absorption Study
inferred← citeshttps://doi.org/10.1002/1521-3773(20010105)40:1<74::aid-anie74>3.0.co;2-copenalex-snapshot
Dendritic Encapsulation of Function: Applying Nature's Site Isolation Principle from Biomimetics to Materials Science
inferred← citeshttps://doi.org/10.1002/1521-3773(20010119)40:2<346::aid-anie346>3.0.co;2-ropenalex-snapshot
Chemically Modified Amino Acids in Copper Proteins That Bind or Activate Dioxygen The author acknowledges the Royal Society (London) for a University Research Fellowship.
inferred← citeshttps://doi.org/10.1002/1521-3773(20010417)40:8<1484::aid-anie1484>3.0.co;2-zopenalex-snapshot
A Short Copper-Copper Distance in a (μ-1,2-Peroxo)dicopper(II) Complex Having a 1,8-Naphthyridine Unit as an Additional Bridge
inferred← citeshttps://doi.org/10.1002/1521-3773(20010803)40:15<2782::aid-anie2782>3.0.co;2-popenalex-snapshot
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins
inferred← citeshttps://doi.org/10.1002/1521-3773(20010803)40:15<2782::aid-anie2782>3.3.co;2-gopenalex-snapshot
Dioxygen Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three Proteins A list of abbreviations can be found in Section 7.
inferred← citeshttps://doi.org/10.1002/1521-3773(20011217)40:24<4570::aid-anie4570>3.0.co;2-4openalex-snapshot
Oxygen Binding, Activation, and Reduction to Water by Copper Proteins
inferred← citeshttps://doi.org/10.1002/1521-3773(20020402)41:7<1114::aid-anie1114>3.0.co;2-6openalex-snapshot
Bis(μ-oxo)dimetal “Diamond” Cores in Copper and Iron Complexes Relevant to Biocatalysis
inferred← citeshttps://doi.org/10.1002/2211-5463.13070openalex-snapshot
Wor1‐regulated ferroxidases contribute to pigment formation in opaque cells of Candida albicans
inferred← citeshttps://doi.org/10.1002/9780470010303.ch4openalex-snapshot
Iron Uptake by Plants and Fungi
inferred← citeshttps://doi.org/10.1002/9780470027318.a9083openalex-snapshot
Electrochemical Detection of Proteins
inferred← citeshttps://doi.org/10.1002/9780470048672.wecb431openalex-snapshot
Oxygen‐Activating Enzymes, Chemistry of
inferred← citeshttps://doi.org/10.1002/9780470054581.eib379openalex-snapshot
Laccase
inferred← citeshttps://doi.org/10.1002/9780470141663.ch10openalex-snapshot
Copper Proteins as Model Systems for Investigating Intramolecular Electron Transfer Processes
inferred← citeshttps://doi.org/10.1002/9780470144428.ch9openalex-snapshot
Bispidine Coordination Chemistry
inferred← citeshttps://doi.org/10.1002/9780470447758.refsopenalex-snapshot
References
inferred← citeshttps://doi.org/10.1002/9780470463772.ch17openalex-snapshot
Electrocatalysis for Fuel Cells at Enzyme‐Modified Electrodes
inferred← citeshttps://doi.org/10.1002/9780470630693.ch2openalex-snapshot
Comparison of Electrocatalysis and Bioelectrocatalysis of Hydrogen and Oxygen Redox Reactions
inferred← citeshttps://doi.org/10.1002/9780470630693.ch5openalex-snapshot
Biocathodes for Dioxygen Reduction in Biofuel Cells
inferred← citeshttps://doi.org/10.1002/9780470661345.smc174openalex-snapshot
Supramolecular Bioinorganic Chemistry
inferred← citeshttps://doi.org/10.1002/9780470682531.pat0467openalex-snapshot
Nitroxyl Radicals
inferred← citeshttps://doi.org/10.1002/9780470682531.pat0602openalex-snapshot
Biological and Biomedical Aspects of Metal Phenolates
inferred← citeshttps://doi.org/10.1002/9780470872390.refsopenalex-snapshot
References
inferred← citeshttps://doi.org/10.1002/9780470974001.f500006openalex-snapshot
Enzyme catalysis in biological fuel cells
inferred← citeshttps://doi.org/10.1002/9781118094365.ch10openalex-snapshot
Supramolecular Copper Dioxygen Chemistry
inferred← citeshttps://doi.org/10.1002/9781118094365.ch4openalex-snapshot
Energy Conversion and Conservation by Cytochrome Oxidases
inferred← citeshttps://doi.org/10.1002/9781118094365.ch5openalex-snapshot
Multicopper Proteins
inferred← citeshttps://doi.org/10.1002/9781118094365.ch7openalex-snapshot
Theoretical Aspects of Dioxygen Activation in Dicopper Enzymes
inferred← citeshttps://doi.org/10.1002/9781118094365.ch8openalex-snapshot
Chemical Reactivity of Copper Active‐Oxygen Complexes
inferred← citeshttps://doi.org/10.1002/9781118271858.ch16openalex-snapshot
Biosensors for Drug Analysis
inferred← citeshttps://doi.org/10.1002/9781118409343.ch1openalex-snapshot
Enzymes Involved in Redox Reactions: Natural Sources and Mechanistic Overview
inferred← citeshttps://doi.org/10.1002/9781118409343.ch5openalex-snapshot
Reactions Involving Oxidases and Peroxidases
inferred← citeshttps://doi.org/10.1002/9781118571811.ch5openalex-snapshot
Rational Design of Protein Cages for Alternative Enzymatic Functions
inferred← citeshttps://doi.org/10.1002/9781118642047.ch10openalex-snapshot
Lignin‐Degrading Enzymes: An Overview
inferred← citeshttps://doi.org/10.1002/9781118690659.ch10openalex-snapshot
Copper‐Mediated Aryl–Aryl Bond Formation Leading to Biaryls: A Century after the Ullmann Breakthrough
inferred← citeshttps://doi.org/10.1002/9781118721001.ch6openalex-snapshot
Use of Fungal Laccases and Peroxidases for Enzymatic Treatment of Wastewater Containing Synthetic Dyes
inferred← citeshttps://doi.org/10.1002/9781118754887.ch14openalex-snapshot
Selective Oxidation of Aromatic Rings
inferred← citeshttps://doi.org/10.1002/9781118802236.ch04openalex-snapshot
Copper Proteins
inferred← citeshttps://doi.org/10.1002/9781118869796.ch03openalex-snapshot
Direct Bioelectrocatalysis: Oxygen Reduction for Biological Fuel Cells
inferred← citeshttps://doi.org/10.1002/9781118869796.ch07openalex-snapshot
Protein Engineering for Enzymatic Fuel Cells
inferred← citeshttps://doi.org/10.1002/9781118869796.ch08openalex-snapshot
Purification and Characterization of Multicopper Oxidases for Enzyme Electrodes
inferred← citeshttps://doi.org/10.1002/9781118869796.ch09openalex-snapshot
Mediated Enzyme Electrodes
inferred← citeshttps://doi.org/10.1002/9781118869796.ch13openalex-snapshot
Imaging and Characterization of The Bio–Nano Interface
inferred← citeshttps://doi.org/10.1002/9781118869796.ch15openalex-snapshot
In SituX‐Ray Spectroscopy of Enzymatic Catalysis: Laccase‐Catalyzed Oxygen Reduction
inferred← citeshttps://doi.org/10.1002/9781118899076.ch8openalex-snapshot
Molecular Properties and Reaction Mechanism of Multicopper Oxidases Related to Their Use in Biofuel Cells
inferred← citeshttps://doi.org/10.1002/9781118925645.ch5openalex-snapshot
Iron Uptake by Plants and Fungi
inferred← citeshttps://doi.org/10.1002/9781118958308.ch5openalex-snapshot
Fungal laccase in the textile industry
inferred← citeshttps://doi.org/10.1002/9781119555384.ch4openalex-snapshot
Current Trends in the Production of Ligninolytic Enzymes
inferred← citeshttps://doi.org/10.1002/9781119735984.ch10openalex-snapshot
Lignin Conversion through Biological and Chemical Routes
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0049openalex-snapshot
Copper: Hemocyanin/Tyrosinase ModelsBased in part on the article Copper: Hemocyanin/Tyrosinase Models by Nobumasa Kitajima which appeared in the Encyclopedia of Inorganic Chemistry, First Edition .
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0049.pub2openalex-snapshot
Copper: Hemocyanin/Tyrosinase Models
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0052openalex-snapshot
Copper Proteins with Dinuclear Active SitesBased in part on the article Copper Proteins with Dinuclear Active Sites by Konrad Lerch which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0053openalex-snapshot
Copper Proteins: Oxidases
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0054openalex-snapshot
Copper Proteins with Type 1 SitesBased in part on the article Copper Proteins with Type 1 Sites by Edward N. Baker which appeared in theEncyclopedia of Inorganic Chemistry, First Edition.
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0375openalex-snapshot
Quantum Mechanical/Molecular Mechanical ( QM / MM ) Methods and Applictions in Bioinorganic Chemistry
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0623openalex-snapshot
Catechol Oxidase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0626openalex-snapshot
Laccase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0659openalex-snapshot
Particulate Methane Monooxygenase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0672openalex-snapshot
Human Factor VIII
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0683openalex-snapshot
Structure, Spectroscopy, and Function of Tyrosinase; Comparison with Hemocyanin and Catechol Oxidase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2249openalex-snapshot
Theoretical Studies on Tyrosinase Models
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2475openalex-snapshot
Multicopper Oxidase Assembly
inferred← citeshttps://doi.org/10.1002/9781394203932.ch10openalex-snapshot
Polyphenols for Sensing/Biosensing Application
inferred← citeshttps://doi.org/10.1002/9783527613700.ch18openalex-snapshot
Dioxygen and alkane activation by iron‐containing enzymes
inferred← citeshttps://doi.org/10.1002/9783527619405.ch5mopenalex-snapshot
Aerobic, Metal‐Catalyzed Oxidation of Alcohols
inferred← citeshttps://doi.org/10.1002/9783527619450.ch9openalex-snapshot
C‐H Transformation at Unfunctionalized Alkanes
inferred← citeshttps://doi.org/10.1002/9783527621620.ch10openalex-snapshot
Laccases–Oxidative Enzymes for Bioremediation of Xenotics and Inactivation of Bacillus Spores
inferred← citeshttps://doi.org/10.1002/9783527621767.ch5openalex-snapshot
Mimicking Nature: Bio‐Inspired Models of Copper Proteins
inferred← citeshttps://doi.org/10.1002/9783527628902.ch5openalex-snapshot
Mimicking Nature: Bio‐Inspired Models of Copper Proteins
inferred← citeshttps://doi.org/10.1002/9783527630516.ch11openalex-snapshot
O 2 Reactivity at Model Copper Systems: Mimicking Tyrosinase Activity
inferred← citeshttps://doi.org/10.1002/9783527630516.ch2openalex-snapshot
The Bioinorganic and Organometallic Chemistry of Copper(III)
inferred← citeshttps://doi.org/10.1002/9783527631421.ch10openalex-snapshot
Polymer Synthesis and Modification by Enzymatic Catalysis
inferred← citeshttps://doi.org/10.1002/9783527633531.ch15openalex-snapshot
Biological Systems
inferred← citeshttps://doi.org/10.1002/9783527673148.ch15openalex-snapshot
Direct‐Electron‐Transfer‐Based Enzymatic Fuel CellsIn Vitro,Ex Vivo, andIn Vivo
inferred← citeshttps://doi.org/10.1002/9783527680603.ch59openalex-snapshot
Fundamental Aspects of Electrocatalysis1)
inferred← citeshttps://doi.org/10.1002/9783527698479.ch6openalex-snapshot
Asymmetric Oxidative Dearomatization Reaction
inferred← citeshttps://doi.org/10.1002/9783527809080.cataz17420openalex-snapshot
tyrosinase
inferred← citeshttps://doi.org/10.1002/9783527823987.vol1_c11openalex-snapshot
Molecular Design of Glucose Biofuel Cell Electrodes
inferred← citeshttps://doi.org/10.1002/9783527830572.ch6openalex-snapshot
Design of PGM ‐free ORR Catalysts: From Molecular to the State of the Art
inferred← citeshttps://doi.org/10.1002/9783527834242.chf0226openalex-snapshot
Contemporary Concepts to Decipher the Reactivity of Paramagnetic Transition Metal Catalysts
inferred← citeshttps://doi.org/10.1002/9783527844340.ch12openalex-snapshot
An Overview of Production of Bacterial and Fungal Laccases and Their Industrial Applications
inferred← citeshttps://doi.org/10.1002/9783527844340.ch32openalex-snapshot
Microbial Laccases: Structure, Function, and Applications
inferred← citeshttps://doi.org/10.1002/adfm.201706319openalex-snapshot
Evidence that Crystal Facet Orientation Dictates Oxygen Evolution Intermediates on Rutile Manganese Oxide
inferred← citeshttps://doi.org/10.1002/adfm.77035openalex-snapshot
Sp‐Carbon–Based Single‐Atom/Nanocluster Laccase‐Mimetic Nanozyme With Three‐Dimensional Separated Active Sites for Regulating Lignin Biosynthesis in Salt‐Stressed Maize Roots
inferred← citeshttps://doi.org/10.1002/adhm.202300327openalex-snapshot
Tyrosinase‐activated Nanocomposites for Double‐Modals Imaging Guided Photodynamic and Photothermal Synergistic Therapy
inferred← citeshttps://doi.org/10.1002/adma.202309098openalex-snapshot
Exploiting the Mechanical Bond Effect for Enhanced Molecular Recognition and Sensing
inferred← citeshttps://doi.org/10.1002/admi.202202065openalex-snapshot
Laccase‐Triggered Surface Co‐Deposition of Gentisic Acid and Chitosan for Multifunctional Polymer Membranes
inferred← citeshttps://doi.org/10.1002/adsc.200505043openalex-snapshot
Significant and Unexpected Solvent Influence on the Selectivity of Laccase‐Catalyzed Coupling of Tetrahydro‐2‐naphthol Derivatives
inferred← citeshttps://doi.org/10.1002/adsc.200505047openalex-snapshot
Biocatalyzed Generation of Molecular Diversity: Selective Modification of the Saponin Asiaticoside
inferred← citeshttps://doi.org/10.1002/adsc.200505216openalex-snapshot
Mild Peroxidative Oxidation of Cyclohexane Catalyzed by Mono‐, Di‐, Tri‐, Tetra‐ and Polynuclear Copper Triethanolamine Complexes
inferred← citeshttps://doi.org/10.1002/adsc.200600557openalex-snapshot
Theoretical Studies on ortho‐Oxidation of Phenols with Dioxygen Mediated by Dicopper Complex: Hints for a Catalyst with the Phenolase Activity of Tyrosinase
inferred← citeshttps://doi.org/10.1002/adsc.200800775openalex-snapshot
Synthetic Applications of Laccase in Green Chemistry
inferred← citeshttps://doi.org/10.1002/adsc.200900271openalex-snapshot
On the Mechanism of Biotransformation of the Anthraquinonic Dye Acid Blue 62 by Laccases
inferred← citeshttps://doi.org/10.1002/adsc.201000456openalex-snapshot
Aerobic Oxidation of Primary Alcohols Catalyzed by Copper Salts and Catalytically Active μ‐Hydroxyl‐Bridged Trinuclear Copper Intermediate
inferred← citeshttps://doi.org/10.1002/adsc.201200162openalex-snapshot
Copper‐Catalyzed Activation of Dioxygen: Oxidative Cyclization of 2‐Arylindoles
inferred← citeshttps://doi.org/10.1002/adsc.201200892openalex-snapshot
From Diols to Lactones under Aerobic Conditions using a Laccase/TEMPO Catalytic System in Aqueous Medium
inferred← citeshttps://doi.org/10.1002/adsc.201400260openalex-snapshot
Laccase/2,2,6,6‐Tetramethylpiperidinoxyl Radical (TEMPO): An Efficient Catalytic System for Selective Oxidations of Primary Hydroxy and Amino Groups in Aqueous and Biphasic Media
inferred← citeshttps://doi.org/10.1002/adsc.201500893openalex-snapshot
Double‐Oxidative Dehydrogenative (DOD) Cyclization of Glycine Derivatives with Dioxane under Metal‐Free Aerobic Conditions
inferred← citeshttps://doi.org/10.1002/adsc.201601066openalex-snapshot
Gold‐Oxazoline Complex‐Catalyzed Cross‐Dehydrogenative Coupling of Glycine Derivatives and Alkenes
inferred← citeshttps://doi.org/10.1002/adsc.201800299openalex-snapshot
Chemo‐Enzymatic Oxidative Rearrangement of Tertiary Allylic Alcohols: Synthetic Application and Integration into a Cascade Process
inferred← citeshttps://doi.org/10.1002/adtp.202300049openalex-snapshot
Copper‐Based Nanomaterials: A Rising Star in Cancer Therapy
inferred← citeshttps://doi.org/10.1002/adtp.202300198openalex-snapshot
Copper‐Related Cell Death and the Role of Copper in Head and Neck Squamous Cell Carcinoma and Therapeutic Strategies
inferred← citeshttps://doi.org/10.1002/aenm.201100433openalex-snapshot
Design of Carbon Nanotube‐Based Gas‐Diffusion Cathode for O2 Reduction by Multicopper Oxidases
inferred← citeshttps://doi.org/10.1002/aenm.202003323openalex-snapshot
Electrocatalytic Oxygen Reduction to Hydrogen Peroxide: From Homogeneous to Heterogeneous Electrocatalysis
inferred← citeshttps://doi.org/10.1002/ajoc.202200564openalex-snapshot
Recent Advances in Molecular Oxygen Assisted Laccase Catalyzed Sustainable Organic Transformations
inferred← citeshttps://doi.org/10.1002/ajoc.70140openalex-snapshot
Transition Metal Catalyst Free Expedient Catechol Oxidation to Quinone via Photocatalysis
inferred← citeshttps://doi.org/10.1002/ange.19971092011openalex-snapshot
Anaerobe Kupfer‐katalysierte Oxidation von Alkoholen zu Aldehyden und Ketonen
inferred← citeshttps://doi.org/10.1002/ange.200353458openalex-snapshot
Effiziente kupferkatalysierte aerobe Oxidation primärer Alkohole
inferred← citeshttps://doi.org/10.1002/ange.200500525openalex-snapshot
Anwendung von Übergangsmetallkomplexen zum Bleichen von Textilien und Holzpulpe
inferred← citeshttps://doi.org/10.1002/ange.200500585openalex-snapshot
Multinuclear Copper Triethanolamine Complexes as Selective Catalysts for the Peroxidative Oxidation of Alkanes under Mild Conditions
inferred← citeshttps://doi.org/10.1002/ange.200501013openalex-snapshot
Alzheimer's Disease Related Copper( II )‐ β‐Amyloid Peptide Exhibits Phenol Monooxygenase and Catechol Oxidase Activities
inferred← citeshttps://doi.org/10.1002/ange.200601255openalex-snapshot
Die erste Kristallstruktur von Tyrosinase: alle Fragen beantwortet?
inferred← citeshttps://doi.org/10.1002/ange.200700604openalex-snapshot
Katalytische Oxidation von organischen Substraten durch molekularen Sauerstoff und Wasserstoffperoxid über einen mehrstufigen Elektronentransfer – ein biomimetischer Ansatz
inferred← citeshttps://doi.org/10.1002/ange.200801364openalex-snapshot
Transistor‐Like Behavior of a Fungal Laccase
inferred← citeshttps://doi.org/10.1002/ange.200901888openalex-snapshot
A Ferromagnetic [Cu3(OH)2]4+ Cluster Formed inside a Tritopic Nonaazapyridinophane: Crystal Structure and Solution Studies
inferred← citeshttps://doi.org/10.1002/ange.200905577openalex-snapshot
Glückszahl Sieben: Charakterisierung stabiler, T‐förmiger Kupfer(II)‐Komplexe von [32]Heptaphyrinen
inferred← citeshttps://doi.org/10.1002/ange.201000973openalex-snapshot
Das erste katalytische Tyrosinasemodell basierend auf einem einkernigen Kupfer(I)‐Komplex: Kinetik und Mechanismus
inferred← citeshttps://doi.org/10.1002/ange.201002106openalex-snapshot
An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein
inferred← citeshttps://doi.org/10.1002/ange.201100219openalex-snapshot
Catalytic and Direct Oxyphosphorylation of Alkenes with Dioxygen and H‐Phosphonates Leading to β‐Ketophosphonates
inferred← citeshttps://doi.org/10.1002/ange.201103945openalex-snapshot
Kupferkatalysierte aerobe oxidative C‐H‐Funktionalisierungen: Trends und Erkenntnisse zum Mechanismus
inferred← citeshttps://doi.org/10.1002/ange.201105285openalex-snapshot
Copper‐Catalyzed Aerobic Oxidative Coupling of Aryl Acetaldehydes with Anilines Leading to α‐Ketoamides
inferred← citeshttps://doi.org/10.1002/ange.201206382openalex-snapshot
Synthesis of Oxazoles through Copper‐Mediated Aerobic Oxidative Dehydrogenative Annulation and Oxygenation of Aldehydes and Amines
inferred← citeshttps://doi.org/10.1002/ange.201208166openalex-snapshot
Refined Distances Between Paramagnetic Centers of a Multi‐Copper Nitrite Reductase Determined by Pulsed EPR (iDEER) Spectroscopy
inferred← citeshttps://doi.org/10.1002/ange.201301249openalex-snapshot
Katalytische Phenolhydroxylierung mit Sauerstoff: Substratvielfalt jenseits der Proteinmatrix von Tyrosinase
inferred← citeshttps://doi.org/10.1002/ange.201301634openalex-snapshot
Aerobic Oxysulfonylation of Alkenes Leading to Secondary and Tertiary β‐Hydroxysulfones
inferred← citeshttps://doi.org/10.1002/ange.201309505openalex-snapshot
Molekulare CuII‐O‐CuII‐Komplexe: Stille Wasser sind tief
inferred← citeshttps://doi.org/10.1002/ange.201311103openalex-snapshot
A Biomimetic Catalytic Aerobic Functionalization of Phenols
inferred← citeshttps://doi.org/10.1002/ange.201403415openalex-snapshot
A Bioinspired Catalytic Oxygenase Cascade to Generate Complex Oxindoles
inferred← citeshttps://doi.org/10.1002/ange.201405060openalex-snapshot
Selective Ortho‐Hydroxylation–Defluorination of 2‐Fluorophenolates with a Bis(μ‐oxo)dicopper(III) Species
inferred← citeshttps://doi.org/10.1002/ange.201406905openalex-snapshot
Auto‐Oxidative Coupling of Glycine Derivatives
inferred← citeshttps://doi.org/10.1002/ange.201508372openalex-snapshot
O2 Activation and Double CH Oxidation by a Mononuclear Manganese(II) Complex
inferred← citeshttps://doi.org/10.1002/ange.201508534openalex-snapshot
Tyrosinase versus Catecholoxidase: ein Asparagin macht den Unterschied
inferred← citeshttps://doi.org/10.1002/ange.201609895openalex-snapshot
Near‐Infrared Fluorescent Probe with New Recognition Moiety for Specific Detection of Tyrosinase Activity: Design, Synthesis, and Application in Living Cells and Zebrafish
inferred← citeshttps://doi.org/10.1002/ange.201805074openalex-snapshot
A Modular Approach for Interlocking Enzymes in Whatman Paper
inferred← citeshttps://doi.org/10.1002/ange.201904075openalex-snapshot
Fast Oxygen Reduction Catalyzed by a Copper(II) Tris(2‐pyridylmethyl)amine Complex through a Stepwise Mechanism
inferred← citeshttps://doi.org/10.1002/ange.201909868openalex-snapshot
Dearomatization of Electron‐Deficient Phenols to ortho‐Quinones: Bidentate Nitrogen‐Ligated Iodine(V) Reagents
inferred← citeshttps://doi.org/10.1002/ange.202102589openalex-snapshot
Redox‐Neutral S‐nitrosation Mediated by a Dicopper Center
inferred← citeshttps://doi.org/10.1002/ange.202111049openalex-snapshot
Synthesis of (±)‐Setigerumine I: Biosynthetic Origins of the Elusive Racemic Papaveraceae Isoxazolidine Alkaloids**
inferred← citeshttps://doi.org/10.1002/ange.202111076openalex-snapshot
Biosynthetic Studies of Phomopsins Unveil Posttranslational Installation of Dehydroamino Acids by UstYa Family Proteins
inferred← citeshttps://doi.org/10.1002/ange.202211016openalex-snapshot
Sustainable Wacker‐Type Oxidations
inferred← citeshttps://doi.org/10.1002/ange.202219034openalex-snapshot
Expanding the Promiscuity of a Copper‐Dependent Oxidase for Enantioselective Cross‐Coupling of Indoles
inferred← citeshttps://doi.org/10.1002/ange.202314019openalex-snapshot
Increasing Reduction Potentials of Type 1 Copper Center and Catalytic Efficiency of Small Laccase from Streptomyces coelicolor through Secondary Coordination Sphere Mutations
inferred← citeshttps://doi.org/10.1002/ange.7825637openalex-snapshot
Biomimetic Synthesis of Multinuclear Metal‐Oxo Bridges Under Mild Aqueous Conditions for Catalytic Cancer Therapy
inferred← citeshttps://doi.org/10.1002/anie.199722081openalex-snapshot
Anaerobic Copper‐Catalyzed Oxidation of Alcohols to Aldehydes and Ketones
inferred← citeshttps://doi.org/10.1002/anie.200353458openalex-snapshot
Efficient, Copper‐Catalyzed, Aerobic Oxidation of Primary Alcohols
inferred← citeshttps://doi.org/10.1002/anie.200500525openalex-snapshot
Applications of Transition‐Metal Catalysts to Textile and Wood‐Pulp Bleaching
inferred← citeshttps://doi.org/10.1002/anie.200500585openalex-snapshot
Multinuclear Copper Triethanolamine Complexes as Selective Catalysts for the Peroxidative Oxidation of Alkanes under Mild Conditions
inferred← citeshttps://doi.org/10.1002/anie.200501013openalex-snapshot
Alzheimer's Disease Related Copper( II )‐ β‐Amyloid Peptide Exhibits Phenol Monooxygenase and Catechol Oxidase Activities
inferred← citeshttps://doi.org/10.1002/anie.200601255openalex-snapshot
The First Crystal Structure of Tyrosinase: All Questions Answered?
inferred← citeshttps://doi.org/10.1002/anie.200700604openalex-snapshot
Catalytic Oxidation of Organic Substrates by Molecular Oxygen and Hydrogen Peroxide by Multistep Electron Transfer—A Biomimetic Approach
inferred← citeshttps://doi.org/10.1002/anie.200801364openalex-snapshot
Transistor‐Like Behavior of a Fungal Laccase
inferred← citeshttps://doi.org/10.1002/anie.200901888openalex-snapshot
A Ferromagnetic [Cu3(OH)2]4+ Cluster Formed inside a Tritopic Nonaazapyridinophane: Crystal Structure and Solution Studies
inferred← citeshttps://doi.org/10.1002/anie.200905577openalex-snapshot
Lucky Seven: Characterization of Stable T‐Shaped Copper(II) Complexes of [32]Heptaphyrins
inferred← citeshttps://doi.org/10.1002/anie.201000973openalex-snapshot
The First Catalytic Tyrosinase Model System Based on a Mononuclear Copper(I) Complex: Kinetics and Mechanism
inferred← citeshttps://doi.org/10.1002/anie.201002106openalex-snapshot
An Artificial Metalloenzyme: Creation of a Designed Copper Binding Site in a Thermostable Protein
inferred← citeshttps://doi.org/10.1002/anie.201100219openalex-snapshot
Catalytic and Direct Oxyphosphorylation of Alkenes with Dioxygen and H‐Phosphonates Leading to β‐Ketophosphonates
inferred← citeshttps://doi.org/10.1002/anie.201103945openalex-snapshot
Copper‐Catalyzed Aerobic Oxidative CH Functionalizations: Trends and Mechanistic Insights
inferred← citeshttps://doi.org/10.1002/anie.201105285openalex-snapshot
Copper‐Catalyzed Aerobic Oxidative Coupling of Aryl Acetaldehydes with Anilines Leading to α‐Ketoamides
inferred← citeshttps://doi.org/10.1002/anie.201206382openalex-snapshot
Synthesis of Oxazoles through Copper‐Mediated Aerobic Oxidative Dehydrogenative Annulation and Oxygenation of Aldehydes and Amines
inferred← citeshttps://doi.org/10.1002/anie.201208166openalex-snapshot
Refined Distances Between Paramagnetic Centers of a Multi‐Copper Nitrite Reductase Determined by Pulsed EPR (iDEER) Spectroscopy
inferred← citeshttps://doi.org/10.1002/anie.201301249openalex-snapshot
Catalytic Phenol Hydroxylation with Dioxygen: Extension of the Tyrosinase Mechanism beyond the Protein Matrix
inferred← citeshttps://doi.org/10.1002/anie.201301634openalex-snapshot
Aerobic Oxysulfonylation of Alkenes Leading to Secondary and Tertiary β‐Hydroxysulfones
inferred← citeshttps://doi.org/10.1002/anie.201309505openalex-snapshot
Molecular CuII‐O‐CuIIComplexes: Still Waters Run Deep
inferred← citeshttps://doi.org/10.1002/anie.201311103openalex-snapshot
A Biomimetic Catalytic Aerobic Functionalization of Phenols
inferred← citeshttps://doi.org/10.1002/anie.201403415openalex-snapshot
A Bioinspired Catalytic Oxygenase Cascade to Generate Complex Oxindoles
inferred← citeshttps://doi.org/10.1002/anie.201405060openalex-snapshot
Selective Ortho‐Hydroxylation–Defluorination of 2‐Fluorophenolates with a Bis(μ‐oxo)dicopper(III) Species
showing the first 200 of 3583
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.