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Functional Analogues of Cytochrome c Oxidase, Myoglobin, and Hemoglobin
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Molecular environment effect on O 2binding to lipidporphyrinatoiron(II) complexes in aqueous media
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A Functional Model of Cytochrome c Oxidase: Thermodynamic Implications
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Application of 3-Quinolinoyl Picket Porphyrins to the Electroreduction of Dioxygen to Water: Mimicking the Active Site of Cytochrome c Oxidase
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Iron Porphyrins as Models of Cytochromec Oxidase
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Self-Organized Lipid-Porphyrin Bilayer Membranes in Vesicular Form: Nanostructure, Photophysical Properties, and Dioxygen Coordination
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Electrocatalytic O2 Reduction by Synthetic Analogues of the Heme/Cu Site of Cytochrome Oxidase Incorporated in a Lipid Film
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Distal Cu Ion Protects Synthetic Heme/Cu Analogues of Cytochrome Oxidase against Inhibition by CO and Cyanide
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Dendritic Iron(II) Porphyrins as Models for Hemoglobin and Myoglobin: Specific Stabilization of O2 Complexes in Dendrimers with H-Bond-Donor Centers
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Cofaciale Bis(metallo)diporphyrine als potentielle molekulare Katalysatoren für Mehrelektronenreduktionen und ‐oxidationen kleiner Moleküle
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Synthetic Hemopolymers for Reversible Binding of Molecular Oxygen
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Iron Twin‐Coronet Porphyrins as Models of Myoglobin and Hemoglobin: Amphibious Electrostatic Effects of Overhanging Hydroxyl Groups for Successful CO/O2 Discrimination
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Metal-Containing Polymeric Materials
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Reactive Oxygen Species in Biological Systems
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Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochromeaa 3 and cytochromebo
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Myoglobin models and steric origins of the discrimination between O2 and CO
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On the significance of hydrogen bonds for the discrimination between CO and O2 by myoglobin
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Flash photolysis of the carbon monoxide compounds of wild-type and mutant variants of cytochrome bo from Escherichia coli
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Cooperative reactions of poly-l-lysine-heme complex with molecular oxygen, carbon monoxide or cyanide ion
inferredcites →https://doi.org/10.1016/0014-5793(82)81262-3openalex-snapshot
Allosteric Effects in Haemoglobin
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Enzyme assays: a practical approach
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CuB promotes both binding and reduction of dioxygen at the heme‐copper binuclear center in the Escherichia coli bo‐type ubiquinol oxidase
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Electrocatalysis of oxygen reduction by water-soluble iron porphyrins
inferredcites →https://doi.org/10.1016/0022-2836(80)90262-4openalex-snapshot
Structure and refinement of oxymyoglobin at 1·6 Å resolution
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The molecular basis of blood diseases
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Catalytic electroreduction of molecular oxygen at glassy carbon electrodes with immobilized iron porphyrins containing zero, one, or four amino groups
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Functional and Structural Analogs of the Dioxygen Reduction Site in Terminal Oxidases
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Enzymatic Reactions in Organic Media
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Proton pumping by cytochrome oxidase: progress, problems and postulates
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Where is ‘outside’ in cytochrome c oxidase and how and when do protons get there?
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Mechanism of proton translocation by cytochrome c oxidase: a new four-stroke histidine cycle11Amino acid residues are numbered according to the subunit I structure of cytochrome aa3 from bovine heart mitochondria.
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A novel scenario for the evolution of haem–copper oxygen reductases
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Cytochrome bd terminal oxidase1All amino acid numbering refers to the E. coli enzyme.1
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Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution
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Rational molecular design of a catalytic site: engineering of catalytic functions to the myoglobin active site framework
inferredcites →https://doi.org/10.1016/s0010-8545(01)00384-8openalex-snapshot
Stereoelectronic factors in CO, NO and O2 binding to heme from vibrational spectroscopy and DFT analysis
inferredcites →https://doi.org/10.1016/s0014-5793(97)00735-7openalex-snapshot
EPR spectroscopy of Escherichia coli cytochrome bo which lacks CuB
inferredcites →https://doi.org/10.1016/s0022-0728(83)80356-8openalex-snapshot
Catalytic electroreduction of molecular oxygen using meso-tetrakis(p-carboxyphenyl)porphinatoiron in water
inferredcites →https://doi.org/10.1016/s0065-2911(08)60123-xopenalex-snapshot
Microbial Anaerobic Respiration
inferredcites →https://doi.org/10.1016/s0065-3233(01)58009-2openalex-snapshot
Posttranslationally modified tyrosines from galactose oxidase and cytochrome C oxidase
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X-ray structure and the reaction mechanism of bovine heart cytochrome c oxidase
inferredcites →https://doi.org/10.1016/s0162-0134(00)00155-0openalex-snapshot
Structures of reaction intermediates of bovine cytochrome c oxidase probed by time-resolved vibrational spectroscopy
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Heme–Cu complexes as oxygen-activating functional models for the active site of cytochrome c oxidase
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Structure of cytochrome c oxidase: a comparison of the bacterial and mitochondrial enzymes
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Hydrogen and deuterium in myoglobin as seen by a neutron structure determination at 1.5 Å resolution
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Cytochrome oxidase in health and disease
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Chemical reactivity of the active site of myoglobin
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Nonideal Electrochemical Behavior of Biomimetic Iron Porphyrins: Interfacial Potential Distribution across Multilayer Films
inferredcites →https://doi.org/10.1021/ar000108jopenalex-snapshot
Is the CO Adduct of Myoglobin Bent, and Does It Matter?
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Positive Allosteric Systems Designed on Dynamic Supramolecular Scaffolds: Toward Switching and Amplification of Guest Affinity and Selectivity
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Synthetic Models for Hemoglobin and Myoglobin
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Control of electron delivery to the oxygen reduction site of cytochrome c oxidase: A role for protons
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Site-directed mutants of the cytochrome bo ubiquinol oxidase of Escherichia coli: Amino acid substitutions for two histidines that are putative CuB ligands
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The gateway to the active site of heme-copper oxidases
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Determination of the Carbon Monoxide Binding Constants of Myoglobin Mutants: Comparison of Kinetic and Equilibrium Methods
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Role of the PR Intermediate in the Reaction of Cytochrome c Oxidase with O2
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Cytochrome c Oxidase: Catalytic Cycle and Mechanisms of Proton Pumping-A Discussion
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Synthetic Heme-Dioxygen Complexes
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Mechanisms of Ligand Recognition in Myoglobin
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Synthetic Models for Heme−Copper Oxidases
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The Molecular Mechanism of Autoxidation for Myoglobin and Hemoglobin: A Venerable Puzzle
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Oxygen Carriers (“Blood Substitutes”)Raison d'Etre, Chemistry, and Some Physiology Blut ist ein ganz besondrer Saft
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Electrochemistry of oxygen reduction. 4. Oxygen to water conversion by iron(II)(tetrakis(N-methyl-4-pyridyl)porphyrin) via hydrogen peroxide
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Effect of axial base on dioxygen and carbon monoxide affinities of iron(II) porphyrins. Imidazole vs. pyridine
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Catalytic pathways for the electroreduction of oxygen by iron tetrakis(4-N-methylpyridyl)porphyrin or iron tetraphenylporphyrin adsorbed on edge plane pyrolytic graphite electrodes
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Biomimetic Studies of Terminal Oxidases: Trisimidazole Picket Metalloporphyrins
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Distal Metal Effects in Cobalt Porphyrins Related to CcO
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Metal-Bridging Mechanism for O−O Bond Cleavage in Cytochrome c Oxidase
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Water-Soluble Polymer-Bound Biomimetic Analogues of Cytochrome c Oxidase Catalyze 4e- Reduction of O2 to Water
inferredcites →https://doi.org/10.1021/ic034488ropenalex-snapshot
Effect of Electron Availability on Selectivity of O2 Reduction by Synthetic Monometallic Fe Porphyrins
inferredcites →https://doi.org/10.1021/ic9600745openalex-snapshot
Interaction of Derivatized Capped Iron(II) Porphyrin Complexes with CO and O2
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Electrocatalytic Activity of Three Iron Porphyrins in the Reductions of Dioxygen and Hydrogen Peroxide at Graphite Electrodes
inferredcites →https://doi.org/10.1021/ja00016a023openalex-snapshot
Structure of a carbon monoxide adduct of a "capped" porphyrin: Fe(C2-Cap)(CO)(1-methylimidazole)
inferredcites →https://doi.org/10.1021/ja00035a028openalex-snapshot
Hydrogen-bonded oxyhemoglobin models with substituted picket-fence porphyrins: the model compound equivalent of site-directed mutagenesis
inferredcites →https://doi.org/10.1021/ja00080a002openalex-snapshot
Dioxygen and carbon monoxide binding to apolar cyclophane hemes: durene-capped hemes
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How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
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Dioxygen Binding in Iron and Cobalt Picnic Basket Porphyrins
inferredcites →https://doi.org/10.1021/ja00105a026openalex-snapshot
Structure-Reactivity Relationship in Oxygen and Carbon Monoxide Binding with Some Heme Models
inferredcites →https://doi.org/10.1021/ja00119a044openalex-snapshot
Conformational Control of Intramolecular Hydrogen Bonding in Heme Models: Maximal CoII-O2 Binding in a C-Clamp Porphyrin
inferredcites →https://doi.org/10.1021/ja00127a017openalex-snapshot
Chemical Models of Hemoglobins and Cytochromes P-450: Influence of the Basicity of the Proximal Ligand on O2 and CO Binding Kinetics
inferredcites →https://doi.org/10.1021/ja0016405openalex-snapshot
Heme/Hydrogen Peroxide Reactivity: Formation of Paramagnetic Iron Oxophlorin Isomers by Treatment of Iron Porphyrins with Hydrogen Peroxide
inferredcites →https://doi.org/10.1021/ja00183a079openalex-snapshot
Structural characterization of a sterically encumbered iron(II) porphyrin carbonyl complex
inferredcites →https://doi.org/10.1021/ja00200a017openalex-snapshot
Hydrogen-bond stabilization of dioxygen: conformation excitation and autoxidation mechanism in hemoprotein models as revealed by oxygen-17 NMR spectroscopy
inferredcites →https://doi.org/10.1021/ja00212a032openalex-snapshot
A deoxymyoglobin model with a sterically unhindered axial imidazole
inferredcites →https://doi.org/10.1021/ja002745aopenalex-snapshot
Modeling Cytochrome Oxidase: A Quantum Chemical Study of the O−O Bond Cleavage Mechanism
inferredcites →https://doi.org/10.1021/ja00282a016openalex-snapshot
Artificial allosteric systems. 4. T/R Characterization of an artificial allosteric system by resonance Raman spectroscopy and oxygen or carbon monoxide affinity
inferredcites →https://doi.org/10.1021/ja00304a021openalex-snapshot
Artificial allosteric systems. 3. Cooperative carbon monoxide binding to diiron(II)-gable porphyrin-diimidazolylmethane complexes
inferredcites →https://doi.org/10.1021/ja00309a014openalex-snapshot
Structural differentiation of carbon monoxide and oxygen binding to iron porphyrins: polar pocket effects
inferredcites →https://doi.org/10.1021/ja00347a066openalex-snapshot
Cooperative dioxygen binding by cobalt(II) gable porphyrin in homogeneous solution
inferredcites →https://doi.org/10.1021/ja00348a019openalex-snapshot
Dioxygen and carbonyl binding to iron(II) porphyrins: a comparison of the "picket fence" and "pocket" porphyrins
inferredcites →https://doi.org/10.1021/ja00528a051openalex-snapshot
Structure of the free-base "capped" porphyrin, 5,10,15,20-[pyrromellitoyl(tetrakis-o-oxyethoxyphenyl)]porphyrin
inferredcites →https://doi.org/10.1021/ja00529a055openalex-snapshot
Models for the active site of oxygen-binding hemoproteins. Dioxygen binding properties and the structures of (2-methylimidazole)-meso-tetra(.alpha.,.alpha.,.alpha.,.alpha.-o-pivalamidophenyl)porphyrinatoiron(II)-ethanol and its dioxygen adduct
inferredcites →https://doi.org/10.1021/ja01538a024openalex-snapshot
Hemoglobin Studies. I. The Combination of Carbon Monoxide with Hemoglobin and Related Model Compounds
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Functional Analogues of the Dioxygen Reduction Site in Cytochrome Oxidase: Mechanistic Aspects and Possible Effects of CuB
inferredcites →https://doi.org/10.1021/ja034382vopenalex-snapshot
Spectroscopic Evidence for a Heme−Superoxide/Cu(I) Intermediate in a Functional Model of Cytochrome c Oxidase
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Structural Characterization of Five Sterically Protected Porphyrins
inferredcites →https://doi.org/10.1021/ja963945iopenalex-snapshot
Aza-Crown-Capped Porphyrin Models of Myoglobin: Studies of the Steric Interactions of Gas Binding
inferredcites →https://doi.org/10.1021/ja983351aopenalex-snapshot
Close Structural Analogues of the Cytochrome c Oxidase Fea3/CuB Center Show Clean 4e- Electroreduction of O2 to H2O at Physiological pH
inferredcites →https://doi.org/10.1021/jo9521615openalex-snapshot
Four-Atom-Linked Capped Porphyrins: Synthesis and Characterization
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Novel Protecting Strategy for the Synthesis of Porphyrins with Different Distal and Proximal Superstructures
inferredcites →https://doi.org/10.1021/jo981835jopenalex-snapshot
Imidazole Acid Chlorides: Preparation and Application in the Syntheses of Biomimetic Heme Models
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Self-Assembled Lipidporphyrin Bilayer Vesicles. Microstructure and Dioxygen Binding in Aqueous Medium
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A Three-Dimensional Model of the Myoglobin Molecule Obtained by X-Ray Analysis
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Structure of Hæmoglobin: A Three-Dimensional Fourier Synthesis at 5.5-Å. Resolution, Obtained by X-Ray Analysis
inferredcites →https://doi.org/10.1038/185422a0openalex-snapshot
Structure of Myoglobin: A Three-Dimensional Fourier Synthesis at 2 Å. Resolution
inferredcites →https://doi.org/10.1038/203182b0openalex-snapshot
Nature of the Iron–Oxygen Bond in Oxyhæmoglobin
inferredcites →https://doi.org/10.1038/292081a0openalex-snapshot
Neutron diffraction reveals oxygen–histidine hydrogen bond in oxymyoglobin
inferredcites →https://doi.org/10.1038/296682a0openalex-snapshot
Molecular rearrangement of mating-type genes in fission yeast
inferredcites →https://doi.org/10.1038/296683a0openalex-snapshot
The iron–oxygen bond in human oxyhaemoglobin
inferredcites →https://doi.org/10.1038/298869a0openalex-snapshot
Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and haemoglobin
inferredcites →https://doi.org/10.1038/35035093openalex-snapshot
A vertebrate globin expressed in the brain
inferredcites →https://doi.org/10.1038/35051719openalex-snapshot
Improving enzymes by using them in organic solvents
inferredcites →https://doi.org/10.1038/356301a0openalex-snapshot
Oxygen activation and the conservation of energy in cell respiration
inferredcites →https://doi.org/10.1038/376660a0openalex-snapshot
Structure at 2.8 Å resolution of cytochrome c oxidase from Paracoccus denitrificans
inferredcites →https://doi.org/10.1038/7586openalex-snapshot
Is cooperative oxygen binding by hemoglobin really understood?
inferredcites →https://doi.org/10.1038/82824openalex-snapshot
The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site.
inferredcites →https://doi.org/10.1038/nsb0494-226openalex-snapshot
Discovery of new ligand binding pathways in myoglobin by random mutagenesis
inferredcites →https://doi.org/10.1039/a800724aopenalex-snapshot
Synthesis and dioxygenation of [5,10,15,20-tetrakis(α,α,α,α-o-pivaloyloxy-naphthyl)porphinato]iron(II) with a covalently bound imidazolylalkyl group
inferredcites →https://doi.org/10.1039/a807598kopenalex-snapshot
New 1,4,7-triazacyclononane-based functional analogues of the Fe/Cu active site of cytochrome c oxidase: structure, spectroscopy and electrocatalytic reduction of oxygen
inferredcites →https://doi.org/10.1039/a903257fopenalex-snapshot
Electrocatalytic reduction of dioxygen to water by tren-capped porphyrins, functional models of cytochrome c oxidase†
inferredcites →https://doi.org/10.1039/a903511gopenalex-snapshot
Kinetics and mechanism of the hydrogen peroxide oxidation of a pentafluorophenyl-substituted iron(III) porphyrin †
inferredcites →https://doi.org/10.1039/b007611mopenalex-snapshot
Synthesis of dendritic iron(II) porphyrins with a tethered axial imidazole ligand designed as new model compounds for globins
inferredcites →https://doi.org/10.1039/b300604bopenalex-snapshot
Substituted tren-capped porphyrins: probing the influence of copper in synthetic models of cytochrome c oxidase
inferredcites →https://doi.org/10.1039/c39830000962openalex-snapshot
Iron( II )‘hanging imidazole’ porphyrin: synthesis and proximal ligand effect on CO and O 2 binding
inferredcites →https://doi.org/10.1039/cc9960001523openalex-snapshot
A dendritic iron porphyrin as a novel haemoprotein mimic: effects of the dendrimer cage on dioxygen-binding activity
inferredcites →https://doi.org/10.1039/dt9930002465openalex-snapshot
Synthesis and dioxygen-binding properties of double-sided porphyrinatoiron(II) complexes bearing covalently bound axial imidazole
inferredcites →https://doi.org/10.1039/p29920000073openalex-snapshot
Influence of polar amide groups upon the kinetics of ligand binding with iron( II ) 5,10,15,20-tetrakis[α,α,α,α-o-(N-tert-butylcarbamoyl)phenyl]porphyrin
inferredcites →https://doi.org/10.1039/p29950000747openalex-snapshot
Synthesis and O 2 -binding properties of tetraphenylporphyrinatoiron( II ) derivatives bearing a proximal imidazole covalently bound at the β-pyrrolic position
inferredcites →https://doi.org/10.1042/bj3240743openalex-snapshot
Comparison of the ligand-binding properties of native and copper-less cytochromes bo from Escherichia coli
inferredcites →https://doi.org/10.1073/pnas.0737308100openalex-snapshot
The role of copper and protons in heme-copper oxidases: Kinetic study of an engineered heme-copper center in myoglobin
inferredcites →https://doi.org/10.1073/pnas.73.10.3333openalex-snapshot
Nature of O2 and CO binding to metalloporphyrins and heme proteins.
inferredcites →https://doi.org/10.1073/pnas.75.3.1052openalex-snapshot
Cooperativity in O2 binding to iron porphyrins.
inferredcites →https://doi.org/10.1073/pnas.89.11.4786openalex-snapshot
Definition of the catalytic site of cytochrome c oxidase: specific ligands of heme a and the heme a3-CuB center.
inferredcites →https://doi.org/10.1073/pnas.96.23.12971openalex-snapshot
How oxygen is activated and reduced in respiration
inferredcites →https://doi.org/10.1073/pnas.98.2.735openalex-snapshot
Myoglobin: A scavenger of bioactive NO
inferredcites →https://doi.org/10.1074/jbc.m112200200openalex-snapshot
The Role of the Cross-link His-Tyr in the Functional Properties of the Binuclear Center in Cytochrome c Oxidase
inferredcites →https://doi.org/10.1074/jbc.m201934200openalex-snapshot
A Ubiquitously Expressed Human Hexacoordinate Hemoglobin
inferredcites →https://doi.org/10.1107/s0108768100005383openalex-snapshot
Crystal structure and charge distribution of YbFeMnO4
inferredcites →https://doi.org/10.1111/j.1748-1716.1954.tb01145.xopenalex-snapshot
Metabolisin of Bone Sodium in Rats Investigated with Na22.
inferredcites →https://doi.org/10.1111/j.1748-1716.1954.tb01149.xopenalex-snapshot
Formation and Elimination of CO in Mammals
inferredcites →https://doi.org/10.1126/science.272.5265.1136openalex-snapshot
The Whole Structure of the 13-Subunit Oxidized Cytochrome c Oxidase at 2.8 Å
inferredcites →https://doi.org/10.1126/science.275.5302.949openalex-snapshot
A Functional Model Related to Cytochrome c Oxidase and Its Electrocatalytic Four-Electron Reduction of O 2
inferredcites →https://doi.org/10.1126/science.290.5496.1588openalex-snapshot
Oxygen Activation and Reduction in Respiration: Involvement of Redox-Active Tyrosine 244
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Ubiquity and Diversity of Dissimilatory (Per)chlorate-Reducing Bacteria
inferredcites →https://doi.org/10.1146/annurev.biophys.27.1.329openalex-snapshot
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What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Oxygen metabolism and a potential role for cytochrome c oxidase in the Warburg effect
inferred← citeshttps://doi.org/10.1007/s11947-026-04375-1openalex-snapshot
Prevention Strategies Toward Discoloration and Spoilage of Fresh Tuna Meat: Alternative Additives and Emerging Technologies
inferred← citeshttps://doi.org/10.1007/s12274-014-0651-4openalex-snapshot
Complex micelles with the bioactive function of reversible oxygen transfer
inferred← citeshttps://doi.org/10.1007/s12678-012-0083-4openalex-snapshot
Reduction Reaction by Porphyrin-Based Catalysts for Fuel Cells
inferred← citeshttps://doi.org/10.1007/s13258-014-0205-xopenalex-snapshot
Proteome alterations of reverse photoperiod-sensitive genic male sterile rice (Oryza sativa L.) at fertility transformation stage
inferred← citeshttps://doi.org/10.1016/b978-0-08-102688-5.00035-0openalex-snapshot
Iron and Manganese Biomimetic Compounds
inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.13356-6openalex-snapshot
Bioinspired Electrocatalysis for the Oxygen Reduction Reaction
inferred← citeshttps://doi.org/10.1016/b978-0-323-88508-9.00003-3openalex-snapshot
Oxygen reduction reaction by metalloporphyrins
inferred← citeshttps://doi.org/10.1016/b978-044452740-0.50013-2openalex-snapshot
Iron: Essential for Almost All Life
inferred← citeshttps://doi.org/10.1016/bs.mie.2016.05.050openalex-snapshot
Design of Heteronuclear Metalloenzymes
inferred← citeshttps://doi.org/10.1016/j.apcata.2006.01.020openalex-snapshot
Copper-2,2′-bipyridines: Catalytic performance and structures in aqueous alkaline solutions
inferred← citeshttps://doi.org/10.1016/j.bbabio.2006.06.005openalex-snapshot
Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations
inferred← citeshttps://doi.org/10.1016/j.bbabio.2009.04.003openalex-snapshot
High resolution crystal structure of Paracoccus denitrificans cytochrome c oxidase: New insights into the active site and the proton transfer pathways
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2021.194687openalex-snapshot
Mechanisms behind polyphagia in a pest insect: Responses of Spodoptera frugiperda (J.E. Smith) strains to preferential and alternative larval host plants assessed with gene regulatory networks
inferred← citeshttps://doi.org/10.1016/j.bbapap.2013.02.031openalex-snapshot
An engineered heme–copper center in myoglobin: CO migration and binding
inferred← citeshttps://doi.org/10.1016/j.bcmd.2007.12.003openalex-snapshot
Heme degradation and oxidative stress in murine models for hemoglobinopathies: Thalassemia, sickle cell disease and hemoglobin C disease
inferred← citeshttps://doi.org/10.1016/j.bcmd.2017.10.006openalex-snapshot
Structure and function of haemoglobins
inferred← citeshttps://doi.org/10.1016/j.biomaterials.2022.121992openalex-snapshot
Cleavable collagenase-assistant nanosonosensitizer for tumor penetration and sonodynamic therapy
inferred← citeshttps://doi.org/10.1016/j.bios.2008.06.009openalex-snapshot
Biofunctional nanocomposite of carbon nanofiber with water-soluble porphyrin for highly sensitive ethanol biosensing
inferred← citeshttps://doi.org/10.1016/j.bios.2014.12.022openalex-snapshot
A label-free electrochemical aptasensor based on the catalysis of manganese porphyrins for detection of thrombin
inferred← citeshttps://doi.org/10.1016/j.bios.2016.07.065openalex-snapshot
A sensitive impedimetric platform biosensing protein: Insoluble precipitates based on the biocatalysis of manganese(III) meso-tetrakis (4-N-methylpyridiniumyl)-porphyrinin in HCR-assisted dsDNA
inferred← citeshttps://doi.org/10.1016/j.blre.2022.100927openalex-snapshot
A new era in oxygen therapeutics? From perfluorocarbon systems to haemoglobin-based oxygen carriers
inferred← citeshttps://doi.org/10.1016/j.carbon.2025.120602openalex-snapshot
A review on the arylation of carbon nanomaterials: fabrication, characterization, and applications in energy storage and conversion devices
inferred← citeshttps://doi.org/10.1016/j.catcom.2015.03.031openalex-snapshot
Synthesis of a porphyrinic polymer for highly efficient oxidation of arylalkanes in water
inferred← citeshttps://doi.org/10.1016/j.cattod.2010.10.084openalex-snapshot
Trinuclear Fe(II)/Ni(II) complexes as catalysts for ethylene polymerizations
inferred← citeshttps://doi.org/10.1016/j.cbpa.2015.01.014openalex-snapshot
High-valent metal-oxo intermediates in energy demanding processes: from dioxygen reduction to water splitting
inferred← citeshttps://doi.org/10.1016/j.cclet.2018.06.002openalex-snapshot
“Pinwheel-like” phthalocyanines with four non-peripheral chiral menthol units: Synthesis, spectroscopy, and electrochemistry
inferred← citeshttps://doi.org/10.1016/j.cclet.2020.03.061openalex-snapshot
Fe, Cu-codoped metal-nitrogen-carbon catalysts with high selectivity and stability for the oxygen reduction reaction
inferred← citeshttps://doi.org/10.1016/j.ccr.2006.08.018openalex-snapshot
Time resolved thermodynamics of ligand binding to heme proteins
inferred← citeshttps://doi.org/10.1016/j.ccr.2007.04.003openalex-snapshot
Recent advances in copper-catalyzed oxidation of organic compounds
inferred← citeshttps://doi.org/10.1016/j.ccr.2012.05.009openalex-snapshot
Resonance Raman characterization of mononuclear heme-peroxo intermediate models
inferred← citeshttps://doi.org/10.1016/j.ccr.2012.06.024openalex-snapshot
X-ray absorption near-edge spectroscopy in bioinorganic chemistry: Application to M–O2 systems
inferred← citeshttps://doi.org/10.1016/j.ccr.2015.04.009openalex-snapshot
Functionality stored in the structures of cyclodextrin–porphyrinoid systems
inferred← citeshttps://doi.org/10.1016/j.ccr.2016.08.008openalex-snapshot
Heme: From quantum spin crossover to oxygen manager of life
inferred← citeshttps://doi.org/10.1016/j.ccr.2017.09.016openalex-snapshot
Metalloporphyrins and related metallomacrocycles as electrocatalysts for use in polymer electrolyte fuel cells and water electrolyzers
inferred← citeshttps://doi.org/10.1016/j.ccr.2019.01.021openalex-snapshot
Tailor made iron porphyrins for investigating axial ligand and distal environment contributions to electronic structure and reactivity
inferred← citeshttps://doi.org/10.1016/j.ccr.2020.213606openalex-snapshot
Synergy between metals for small molecule activation: Enzymes and bio-inspired complexes
inferred← citeshttps://doi.org/10.1016/j.ccr.2023.215496openalex-snapshot
Coordination-driven electrocatalysts as an evolving wave of enthusiasm for sustainable hydrogen production
inferred← citeshttps://doi.org/10.1016/j.checat.2024.101069openalex-snapshot
Selective electrochemical H2O2 production by a molecular copper catalyst: A crucial relation between reaction rate and mass transport
inferred← citeshttps://doi.org/10.1016/j.chembiol.2008.03.018openalex-snapshot
Polyvalent Display of Heme on Hepatitis B Virus Capsid Protein through Coordination to Hexahistidine Tags
inferred← citeshttps://doi.org/10.1016/j.crci.2004.12.001openalex-snapshot
Biological coordination chemistry, a confluence of chemistry and biochemistry
inferred← citeshttps://doi.org/10.1016/j.elecom.2009.08.022openalex-snapshot
Electrochemical evidence of catalysis of oxygen reduction at the polarized liquid–liquid interface by tetraphenylporphyrin monoacid and diacid
inferred← citeshttps://doi.org/10.1016/j.elecom.2019.01.020openalex-snapshot
Stepwise electrocatalytic reduction of nitric oxide by cationic picket-fence porphyrin in an ultrathin phospholipid film
inferred← citeshttps://doi.org/10.1016/j.electacta.2011.01.060openalex-snapshot
Porphyrin-functionalized gold nanoparticles for selective electrochemical detection of peroxyacetic acid
inferred← citeshttps://doi.org/10.1016/j.electacta.2012.03.129openalex-snapshot
Thermodynamic driving force effects in the oxygen reduction catalyzed by a metal-free porphyrin
inferred← citeshttps://doi.org/10.1016/j.electacta.2012.03.132openalex-snapshot
Hydrogen peroxide as a sustainable energy carrier: Electrocatalytic production of hydrogen peroxide and the fuel cell
inferred← citeshttps://doi.org/10.1016/j.electacta.2012.08.002openalex-snapshot
Bionic catalysis of porphyrin for electrochemical detection of nucleic acids
inferred← citeshttps://doi.org/10.1016/j.eurpolymj.2012.09.011openalex-snapshot
Fluorescent chemosensor for the detection of histamine based on dendritic porphyrin-incorporated nanofibers
inferred← citeshttps://doi.org/10.1016/j.fct.2013.08.074openalex-snapshot
Biological importance of reactive oxygen species in relation to difficulties of treating pathologies involving oxidative stress by exogenous antioxidants
inferred← citeshttps://doi.org/10.1016/j.foodchem.2017.06.092openalex-snapshot
Mechanisms and kinetics of heme iron nitrosylation in an in vitro gastro-intestinal model
inferred← citeshttps://doi.org/10.1016/j.ica.2007.08.016openalex-snapshot
Intermolecular versus intramolecular electron-/atom- (Cl ) transfer in heme-iron and copper pyridylalkylamine complexes
inferred← citeshttps://doi.org/10.1016/j.ica.2010.03.026openalex-snapshot
Spectroscopic and electrochemical studies of novel model compounds for cytochrome c oxidase
inferred← citeshttps://doi.org/10.1016/j.ica.2011.12.053openalex-snapshot
β-Tetrakis(2-thienyl)-meso-tetraphenylporphyrins: Synthesis, structural and electrochemical redox properties
inferred← citeshttps://doi.org/10.1016/j.ica.2012.08.007openalex-snapshot
Synthesis and characterization of binuclear Co(II) complexes with bis(salen-type) ligands
inferred← citeshttps://doi.org/10.1016/j.ica.2013.06.026openalex-snapshot
Novel nitrothien-2-ylporphyrins: Spectroscopic and electrochemical investigation on the role of conformation of porphyrins in their reactions
inferred← citeshttps://doi.org/10.1016/j.ica.2017.04.052openalex-snapshot
A question of flexibility in cytochrome c oxidase models
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