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Dissimilatory Nitrite and Nitric Oxide Reductases
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Reductive Disproportionation of NO Mediated by Copper Complexes: Modeling N2O Generation by Copper Proteins and Heterogeneous Catalysts
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Novel Copper Nitrosyl Complexes: Contributions to the Understanding of Dissimilatory, Copper‐Containing Nitrite Reductases
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Expression of the Fungal Cytochrome P450nor cDNA in Escherichia coli
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Characterization of Interactions of Nitric Oxide with Human Hemoglobin A by Infrared Spectroscopy
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Crystallization and Preliminary X-ray Diffraction Studies of Nitric Oxide Reductase Cytochrome P450nor from Fusarium oxysporum
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Catalytic Dehydrogenative Polymerization of Silanes to Polysilanes by Zirconocene and Hafnocene Catalysts. A New Polymerization Mechanism
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Periplasmic location of nitrous oxide reductase and its apoform in denitrifying Pseudomonas stutzeri
inferredcites →https://doi.org/10.1007/bf00258141openalex-snapshot
Copper-containing nitrite reductase from Pseudomonas aureofaciens is functional in a mutationally cytochrome cd 1-free background (NirS−) of Pseudomonas stutzeri
inferredcites →https://doi.org/10.1007/bf00269855openalex-snapshot
Close linkage in Pseudomonas stutzeri of the structural genes for respiratory nitrite reductase and nitrous oxide reductase, and other essential genes for denitrification
inferredcites →https://doi.org/10.1007/bf00292074openalex-snapshot
The biological role of nitric oxide in bacteria
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On the purification of nitrite reductase from Thiobacillus denitrificans and its reaction with nitrite under reducing conditions
inferredcites →https://doi.org/10.1016/0006-291x(80)91184-5openalex-snapshot
Membrane-bound glutathione peroxidase-like activity in mitochondria
inferredcites →https://doi.org/10.1016/0006-291x(89)91820-2openalex-snapshot
Spectroscopic evidence for a copper-nitrosyl intermediate in nitrite reduction by blue copper-containing nitrite reductase
inferredcites →https://doi.org/10.1016/0006-291x(92)90476-2openalex-snapshot
Evidence that the Type 2 copper centers are the site of nitrite reduction by Achromobacter cycloclastes nitrite reductase
inferredcites →https://doi.org/10.1016/0006-291x(92)91600-uopenalex-snapshot
Molecular cloning and sequencing of the gene encoding human angiotensin II type 1 receptor
inferredcites →https://doi.org/10.1016/0006-3002(61)90442-5openalex-snapshot
A nitrite reducing system reconstructed with purified cytochrome components of Pseudomonas aeruginosa
inferredcites →https://doi.org/10.1016/0014-5793(75)80082-2openalex-snapshot
The nitric oxide compounds of Pseudomonas aeruginosa nitrite reductase and their probable participation in the nitrite reduction
inferredcites →https://doi.org/10.1016/0014-5793(82)80383-9openalex-snapshot
The chemical mechanism of microbioal denitrification
inferredcites →https://doi.org/10.1016/0014-5793(89)80998-6openalex-snapshot
Synthesis of spin‐labeled 2‐azido‐ATP: Evidence for distinct nucleotide‐binding sites in calcium pump protein from sarcoplasmic reticulum
inferredcites →https://doi.org/10.1016/0014-5793(89)81004-xopenalex-snapshot
Nitrite reductase from Pseudomonas aeruginosa: Sequence of the gene and the protein
inferredcites →https://doi.org/10.1016/0014-5793(91)80150-2openalex-snapshot
The nirSTBM region coding for cytochrome cd1‐dependent nitrite respiration of Pseudomonas stutzeri consists of a cluster of mono‐, di‐, and tetraheme proteins
inferredcites →https://doi.org/10.1016/0014-5793(91)80237-wopenalex-snapshot
Highly conserved sequences in the 3′‐untranslated region of the COL1A1 gene bind cell‐specific nuclear proteins
inferredcites →https://doi.org/10.1016/0014-5793(91)81099-topenalex-snapshot
Evidence for an NO‐rebound, mechanism for production of N2O from nitrite by the copper‐containing nitrite reductase from Achromobacter cycloclastes
inferredcites →https://doi.org/10.1016/0014-5793(94)80228-9openalex-snapshot
Cytochrome oxidase evolved by tinkering with denitrification enzymes
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(89)90521-4openalex-snapshot
λ Repressor mutants that are better substrates for RecA-mediated cleavage
inferredcites →https://doi.org/10.1016/0031-9422(88)87011-0openalex-snapshot
Immunological patterns of distribution of bacterial denitrifying enzymes
inferredcites →https://doi.org/10.1016/0038-0717(87)90080-0openalex-snapshot
Nitrous oxide sources in aerobic soils: Nitrification, denitrification and other biological processes
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The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1
inferredcites →https://doi.org/10.1016/0378-1097(92)90643-3openalex-snapshot
Denitrification by fungi
inferredcites →https://doi.org/10.1016/0922-338x(93)90061-copenalex-snapshot
Cloning and sequencing of a gene encoding nitrite reductase from Paracoccus denitrificans and expression of the gene in Escherichia coli
inferredcites →https://doi.org/10.1016/0923-2508(89)90030-2openalex-snapshot
Biology of anaerobic microorganisms
inferredcites →https://doi.org/10.1016/s0006-291x(05)80287-6openalex-snapshot
Oxidation of dithiothreitol during turnover of nitric oxide reductase: evidence for generation of nitroxyl with the enzyme from Paracoccus denitrificans
inferredcites →https://doi.org/10.1016/s0006-291x(84)80228-4openalex-snapshot
Patterns of product inhibition for bacterial nitrite reductase
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Electron paramagnetic resonance study of the interaction of some anionic ligands with oxidized Pseudomonas cytochrome oxidase.
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Electron transfer across the chromaffin granule membrane.
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EPR study of heme x NO complexes of ascorbic acid-reduced Pseudomonas cytochrome oxidase and corresponding model complexes.
inferredcites →https://doi.org/10.1016/s0021-9258(18)52464-9openalex-snapshot
Human hexokinase type I microheterogeneity is due to different amino-terminal sequences.
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Cytochrome P-450 55A1 (P-450dNIR) acts as nitric oxide reductase employing NADH as the direct electron donor.
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Detection and modulation in vivo of helix-loop-helix protein-protein interactions.
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Nitric oxide reductase. Purification from Paracoccus denitrificans with use of a single column and some characteristics
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Denitrification by the fungus Fusarium oxysporum and involvement of cytochrome P-450 in the respiratory nitrite reduction
inferredcites →https://doi.org/10.1016/s0021-9258(19)38466-2openalex-snapshot
The reaction of Pseudomonas nitrite reductase and nitrite. A stopped-flow and EPR study.
inferredcites →https://doi.org/10.1016/s0021-9258(20)89474-5openalex-snapshot
Purification of cytochrome cd1 nitrite reductase from Pseudomonas stutzeri JM300 and reconstitution with native and synthetic heme d1.
inferredcites →https://doi.org/10.1021/ar50085a004openalex-snapshot
Coordination chemistry of nitric oxide
inferredcites →https://doi.org/10.1021/ar50085a005openalex-snapshot
Molecular fragments or chemical bonds
inferredcites →https://doi.org/10.1021/bi00028a014openalex-snapshot
Iron-Ligand Structure and Iron Redox Property of Nitric Oxide Reductase Cytochrome P450nor from Fusarium oxysporum: Relevance to Its NO Reduction Activity
inferredcites →https://doi.org/10.1021/bi00177a005openalex-snapshot
EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Alcaligenes xylosoxidans (NCIMB 11015)
inferredcites →https://doi.org/10.1021/bi00183a030openalex-snapshot
X-ray Structure and Site-Directed Mutagenesis of a Nitrite Reductase from Alcaligenes Faecalis S-6: Roles of Two Copper Atoms in Nitrite Reduction
inferredcites →https://doi.org/10.1021/bi00243a020openalex-snapshot
Amino acid sequence of nitrite reductase: a copper protein from Achromobacter cycloclastes
inferredcites →https://doi.org/10.1021/ed062p53openalex-snapshot
Thermodynamic internal energy of an ideal gas of rigid rotors
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A model for the substrate adduct of copper nitrite reductase and its conversion to a novel tetrahedral copper(II) triflate complex
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Dioxygen and carbon monoxide binding to apolar cyclophane hemes: durene-capped hemes
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Evidence for a copper-nitrosyl intermediate in denitrification by the copper-containing nitrite reductase of Achromobacter cycloclastes
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Reduction of nitrate and nitrite in water by immobilized enzymes
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Oplophorus oxyluciferin and a model luciferin compound biologically active with Oplophorus luciferase
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The reactions of Pseudomonas cytochrome c-551 oxidase with potassium cyanide
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Electron paramagnetic resonance studies on Pseudomonas nitrosyl nitrite reductase. Evidence for multiple species in the electron paramagnetic resonance spectra of nitrosyl haemoproteins
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An investigation of the ligand-binding properties of Pseudomonas aeruginosa nitrite reductase
inferredcites →https://doi.org/10.1074/jbc.270.4.1617openalex-snapshot
Spectroscopic and Kinetic Studies on Reaction of Cytochrome P450nor with Nitric Oxide
inferredcites →https://doi.org/10.1074/jbc.270.46.27458openalex-snapshot
The Structure of Copper-nitrite Reductase from Achromobacter cycloclastes at Five pH Values, with NO-2 Bound and with Type II Copper Depleted
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Purification and Properties of a Cyotchrome P-450 of a Fungus, Fusarium oxysporum
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Type 1, blue copper proteins constitute a respiratory nitrite‐reducing system in Pseudomonas aureofaciens
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Synovial protein kinase C and its apparent insensitivity to interleukin‐1
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Bacterial nitrite‐reducing enzymes
inferredcites →https://doi.org/10.1111/j.1432-1033.1994.tb19962.xopenalex-snapshot
Nitric oxide reductase from Pseudomonas stutzeri
inferredcites →https://doi.org/10.1111/j.1574-6968.1992.tb05086.xopenalex-snapshot
Co-denitrification by the denitrifying system of the fungusFusarium oxysporum
inferredcites →https://doi.org/10.1111/j.1574-6968.1994.tb07067.xopenalex-snapshot
The heme-copper oxidase family consists of three distinct types of terminal oxidases and is related to nitric oxide reductase
inferredcites →https://doi.org/10.1126/science.1281928openalex-snapshot
Biochemistry of Nitric Oxide and Its Redox-Activated Forms
inferredcites →https://doi.org/10.1126/science.1862344openalex-snapshot
The 2.3 Angstrom X-Ray Structure of Nitrite Reductase from Achromobacter cycloclastes
inferredcites →https://doi.org/10.1126/science.232.4746.24openalex-snapshot
Why Dynamiting Vampire Bats Is Wrong
inferredcites →https://doi.org/10.1126/science.232.4758.1623openalex-snapshot
Atmospheric Trace Gases: Trends and Distributions Over the Last Decade
inferredcites →https://doi.org/10.1126/science.253.5015.42openalex-snapshot
Celestial Mechanics on a Microscopic Scale
inferredcites →https://doi.org/10.1126/science.270.5233.59openalex-snapshot
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inferredcites →https://doi.org/10.1128/aem.55.11.2924-2931.1989openalex-snapshot
Immunological identification and distribution of dissimilatory heme cd1 and nonheme copper nitrite reductases in denitrifying bacteria
inferredcites →https://doi.org/10.1128/aem.57.8.2403-2407.1991openalex-snapshot
Biodegradation of monoaromatic hydrocarbons by aquifer microorganisms using oxygen, nitrate, or nitrous oxide as the terminal electron acceptor
inferredcites →https://doi.org/10.1128/aem.58.1.376-384.1992openalex-snapshot
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inferredcites →https://doi.org/10.1128/jb.106.2.356-361.1971openalex-snapshot
Separate Nitrite, Nitric Oxide, and Nitrous Oxide Reducing Fractions from Pseudomonas perfectomarinus
inferredcites →https://doi.org/10.1128/jb.171.6.3288-3297.1989openalex-snapshot
Formation of the N-N bond from nitric oxide by a membrane-bound cytochrome bc complex of nitrate-respiring (denitrifying) Pseudomonas stutzeri
inferredcites →https://doi.org/10.1128/jb.172.5.2558-2562.1990openalex-snapshot
Localization of the cytochrome cd1 and copper nitrite reductases in denitrifying bacteria
inferredcites →https://doi.org/10.1128/jb.174.1.8-16.1992openalex-snapshot
The rcsA gene of Escherichia coli O9:K30:H12 is involved in the expression of the serotype-specific group I K (capsular) antigen
inferredcites →https://doi.org/10.1146/annurev.mi.42.100188.001311openalex-snapshot
The Enzymes Associated With Denitrification
inferredcites →https://doi.org/10.1246/bcsj.67.138openalex-snapshot
Direct Electrochemistry of Nitrite Reductase from Achromobacter cycloclastes IAM 1013
inferredcites →https://doi.org/10.5860/choice.26-3877openalex-snapshot
Biology of anaerobic microorganisms
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
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Strong Electron Donor Enables High-Efficient Electrochemical Nitrate Reduction to Ammonia Via Novel Dissociation Pathway
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Interactions of nitric oxide and organic nitroso compounds with metalloporphyrins and heme
inferred← citeshttps://doi.org/10.1002/0470028637.met130openalex-snapshot
Cytochrome cd 1Nitrite Reductase
inferred← citeshttps://doi.org/10.1002/0470862106.ia295openalex-snapshot
Copper Enzymes in Denitrification
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[Ru(HNO)(′pybuS4′)], the First HNO Complex Resulting from Hydride Addition to a NO Complex (′pybuS4′2−=2,6-Bis(2-mercapto- 3,5-di-tert-butylphenylthio)dimethylpyridine(2−))
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Iron Carbonyl, Nitrosyl, and Nitro Complexes of a Tetrapodal Pentadentate Amine Ligand: Synthesis, Electronic Structure, and Nitrite Reductase-like Reactivity
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Inorganic Chemistry in Biology
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Interactions of Nitrosoalkanes/arenes, Nitrosamines, Nitrosothiols, and Alkyl Nitrites with Metals
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Copper Enzymes in Denitrification
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0557openalex-snapshot
Cytochrome cd 1Nitrite Reductase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2119openalex-snapshot
Copper(I) ATPases : Transport Mechanism and Cellular Functions in Bacteria
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2772openalex-snapshot
CytochromecFused Copper Nitrite Reductases
inferred← citeshttps://doi.org/10.1002/9783527610426.bard090006openalex-snapshot
Electrochemistry of Metalloporphyrins in Nonaqueous Media
inferred← citeshttps://doi.org/10.1002/adhm.202403468openalex-snapshot
Advances in Electrochemical Nitrite Reduction toward Nitric Oxide Synthesis for Biomedical Applications
inferred← citeshttps://doi.org/10.1002/adma.202403053openalex-snapshot
Room Temperature Reduction of Nitrogen Oxide on Iron Metal–Organic Frameworks
inferred← citeshttps://doi.org/10.1002/ange.200503555openalex-snapshot
Spectroscopic Characterization of Reaction Intermediates in a Model for Copper Nitrite Reductase
inferred← citeshttps://doi.org/10.1002/ange.200602963openalex-snapshot
The Structure of the Hyponitrite Species in a Heme FeCu Binuclear Center
inferred← citeshttps://doi.org/10.1002/ange.201208063openalex-snapshot
Preparation of the Elusive [(por)Fe(NO)(O‐ligand)] Complex by Diffusion of Nitric Oxide into a Crystal of the Precursor
inferred← citeshttps://doi.org/10.1002/ange.201608539openalex-snapshot
HNO‐Binding in Heme Proteins: Effects of Iron Oxidation State, Axial Ligand, and Protein Environment
inferred← citeshttps://doi.org/10.1002/ange.201807699openalex-snapshot
Mechanisms of HNO Reactions with Ferric Heme Proteins
inferred← citeshttps://doi.org/10.1002/ange.201904732openalex-snapshot
Four‐Coordinate Copper Halonitrosyl {CuNO}10 Complexes
inferred← citeshttps://doi.org/10.1002/ange.202314978openalex-snapshot
Uncovering Nitrosyl Reactivity at N‐Heterocyclic Carbene Center
inferred← citeshttps://doi.org/10.1002/ange.202501338openalex-snapshot
Electronically Asynchronous Transition State Tuned from Remote Site for Oxygen Atom Transfer by Cu II –Nitrite Complexes
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Bioelectrosynthesis of Signaling Molecules for Selective Modulation of Cell Signaling
inferred← citeshttps://doi.org/10.1002/anie.200503555openalex-snapshot
Spectroscopic Characterization of Reaction Intermediates in a Model for Copper Nitrite Reductase
inferred← citeshttps://doi.org/10.1002/anie.200602963openalex-snapshot
The Structure of the Hyponitrite Species in a Heme FeCu Binuclear Center
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Preparation of the Elusive [(por)Fe(NO)(O‐ligand)] Complex by Diffusion of Nitric Oxide into a Crystal of the Precursor
inferred← citeshttps://doi.org/10.1002/anie.201608539openalex-snapshot
HNO‐Binding in Heme Proteins: Effects of Iron Oxidation State, Axial Ligand, and Protein Environment
inferred← citeshttps://doi.org/10.1002/anie.201807699openalex-snapshot
Mechanisms of HNO Reactions with Ferric Heme Proteins
inferred← citeshttps://doi.org/10.1002/anie.201904732openalex-snapshot
Four‐Coordinate Copper Halonitrosyl {CuNO}10 Complexes
inferred← citeshttps://doi.org/10.1002/anie.202314978openalex-snapshot
Uncovering Nitrosyl Reactivity at N‐Heterocyclic Carbene Center
inferred← citeshttps://doi.org/10.1002/anie.202501338openalex-snapshot
Electronically Asynchronous Transition State Tuned from Remote Site for Oxygen Atom Transfer by Cu II –Nitrite Complexes
inferred← citeshttps://doi.org/10.1002/anie.202508192openalex-snapshot
Bioelectrosynthesis of Signaling Molecules for Selective Modulation of Cell Signaling
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Synthesis of Iron Porphyrin with Pendant Thiol Groups: Progress Toward a Model of the Heme/Cu Active Site of Sulfite Reductase
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Nitrite reduction: a ubiquitous function from a pre‐aerobic past
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Remote Water‐Mediated Proton Transfer Triggers Inter‐Cu Electron Transfer: Nitrite Reduction Activation in Copper‐Containing Nitrite Reductase
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Oxidative Homolysis of a Nitrosylchromium Complex
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Fluorescence Lifetime Analysis of Nitrite Reductase from Alcaligenes xylosoxidans at the Single‐Molecule Level Reveals the Enzyme Mechanism
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Copper‐Containing Nitrite Reductase Employing Proton‐Coupled Spin‐Exchanged Electron‐Transfer and Multiproton Synchronized Transfer to Reduce Nitrite
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Acid‐catalyzed Transformation of Nitrite to Nitric Oxide on Copper(II)−Cobalt(II) Centers in a Bimetallic Complex
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One‐Electron NO to N2O Pathways via Heme Models and Lewis Acid: Metal Effects and Differences from the Enzymatic Reaction
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ChemInform Abstract: Dissimilatory Nitrite and Nitric Oxide Reductases
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Enzymatic Bioelectrosynthetic Ammonia Production: Recent Electrochemistry of Nitrogenase, Nitrate Reductase, and Nitrite Reductase
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Nitric Oxide Reduction by Heme‐Thiolate Enzymes (P450nor): A Reevaluation of the Mechanism
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EPR Insensitivity of the Metal‐Nitrosyl Spin‐Bearing Moiety in Complexes [LnRuII‐NO·]k
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Mechanism of Reduction of the Nitrite Ion by CuI Complexes
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Mechanistic Information on the Reversible Binding of NO to Mono‐ and Dinuclear FeII Complexes of a Biomimetic S4N Ligand
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De Novo Designed Copper α‐Helical Peptides: From Design to Function
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Room‐Temperature Catalytic Reduction of Aqueous Nitrate to Ammonia with Ni Nanoparticles Immobilized on an Fe3O4@n‐SiO2@h‐SiO2–NH2 Support
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Fifty Years of Inorganic Biomimetic Chemistry: From the Complexation of Single Metal Cations to Polynuclear Metal Complexes by Multidentate Thiolate Ligands
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A Nitrite Biosensor Based on Coimmobilization of Nitrite Reductase and Viologen‐Modified Polysiloxane on Glassy Carbon Electrode
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Using Biosynthetic Models of Heme‐Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities
inferred← citeshttps://doi.org/10.1002/jcc.20567openalex-snapshot
Elucidating the mechanism for the reduction of nitrite by copper nitrite reductase—A contribution from quantum chemical studies
inferred← citeshttps://doi.org/10.1002/rcm.1586openalex-snapshot
Is the isotopic composition of nitrous oxide an indicator for its origin from nitrification or denitrification? A theoretical approach from referred data and microbiological and enzyme kinetic aspects
inferred← citeshttps://doi.org/10.1002/rcm.3249openalex-snapshot
Oxygen exchange between (de)nitrification intermediates and H 2 O and its implications for source determination of NO and N 2 O: a review
inferred← citeshttps://doi.org/10.1002/rcm.3820openalex-snapshot
Isotopologue fractionation during N 2 O production by fungal denitrification
inferred← citeshttps://doi.org/10.1006/bbrc.1998.8457openalex-snapshot
Cytochrome c Oxidase Does Not Catalyze the Anaerobic Reduction of NO
inferred← citeshttps://doi.org/10.1006/bbrc.1998.8847openalex-snapshot
The Covalent Structure of the Blue Copper-Containing Nitrite Reductase fromAchromobacter xylosoxidans
inferred← citeshttps://doi.org/10.1006/bbrc.1998.9451openalex-snapshot
Roles of Four Iron Centers inParacoccus halodenitrificansNitric Oxide Reductase
inferred← citeshttps://doi.org/10.1006/bbrc.1998.9932openalex-snapshot
Cloning, Sequencing, and Transcriptional Studies of the Gene Encoding Copper-Containing Nitrite Reductase fromAlcaligenes xylosoxidansNCIMB 11015
inferred← citeshttps://doi.org/10.1006/bbrc.2002.6391openalex-snapshot
Cyanide Binding to cd1 Nitrite Reductase from Pseudomonas aeruginosa: Role of the Active-Site His369 in Ligand Stabilization
inferred← citeshttps://doi.org/10.1006/jmbi.1999.2648openalex-snapshot
Structural and kinetic evidence for an ordered mechanism of copper nitrite reductase
inferred← citeshttps://doi.org/10.1006/jmbi.2001.5253openalex-snapshot
Electron donation between copper containing nitrite reductases and cupredoxins: the nature of protein-protein interaction in complex formation 1 1Edited by R. Huber
inferred← citeshttps://doi.org/10.1007/0-306-46828-x_15openalex-snapshot
Cytochrome cd 1 Nitrite Reductase Structure Raises Interesting Mechanistic Questions
inferred← citeshttps://doi.org/10.1007/0-306-47816-1_2openalex-snapshot
Copper-dioxygen complexes and their roles in biomimetic oxidation reactions
inferred← citeshttps://doi.org/10.1007/430_2012_86openalex-snapshot
Biomimetic Chemistry with Tris(triazolyl)borate Ligands: Unique Structures and Reactivity via Interactions with the Remote Nitrogens
inferred← citeshttps://doi.org/10.1007/430_2013_102openalex-snapshot
Coordination Chemistry of Nitrosyls and Its Biochemical Implications
inferred← citeshttps://doi.org/10.1007/430_2013_92openalex-snapshot
Structure and Bonding in Heme–Nitrosyl Complexes and Implications for Biology
inferred← citeshttps://doi.org/10.1007/430_2013_93openalex-snapshot
Synthetic Models of Copper–Nitrosyl Species Proposed as Intermediates in Biological Denitrification
inferred← citeshttps://doi.org/10.1007/978-0-387-28430-9_4openalex-snapshot
Biomimetic NOx Reductions by Heme Models and Proteins
inferred← citeshttps://doi.org/10.1007/978-3-030-71206-8_20openalex-snapshot
Fungi and Nitrogen Cycle: Symbiotic Relationship, Mechanism and Significance
inferred← citeshttps://doi.org/10.1007/978-3-319-13242-6_134openalex-snapshot
Femtosecond Vibrational Spectroscopic Study on Photoexcitation Dynamics of DNO-Bound Myoglobin
inferred← citeshttps://doi.org/10.1007/978-3-319-24945-2_23openalex-snapshot
Algal Physiology and Large-Scale Outdoor Cultures of Microalgae
inferred← citeshttps://doi.org/10.1007/978-94-011-5133-7_13openalex-snapshot
The Chemistry of Biological Denitrification
inferred← citeshttps://doi.org/10.1007/bf02904510openalex-snapshot
Allosteric control of internal electron transfer in cytochromecd 1 nitrite reductase
inferred← citeshttps://doi.org/10.1007/bfb0103376openalex-snapshot
Evolutionary aspects of copper binding centers in copper proteins
inferred← citeshttps://doi.org/10.1007/s00018-007-7310-9openalex-snapshot
Type-2 copper-containing enzymes
inferred← citeshttps://doi.org/10.1007/s00775-006-0078-9openalex-snapshot
Using synthetic chemistry to understand copper protein active sites: a personal perspective
inferred← citeshttps://doi.org/10.1007/s00775-007-0223-0openalex-snapshot
Computational modeling of factors that modulate the unique FeNO bonding in {FeNO}6 heme–thiolate model complexes
inferred← citeshttps://doi.org/10.1007/s00775-008-0349-8openalex-snapshot
Ambidentate H-bonding by heme-bound NO: structural and spectral effects of –O versus –N H-bonding
inferred← citeshttps://doi.org/10.1007/s00775-010-0739-6openalex-snapshot
Substrate binding and activation in the active site of cytochrome c nitrite reductase: a density functional study
inferred← citeshttps://doi.org/10.1007/s00775-016-1398-zopenalex-snapshot
CO and NO bind to Fe(II) DiGeorge critical region 8 heme but do not restore primary microRNA processing activity
inferred← citeshttps://doi.org/10.1007/s10705-017-9901-7openalex-snapshot
Fungal and bacterial contributions to codenitrification emissions of N2O and N2 following urea deposition to soil
inferred← citeshttps://doi.org/10.1007/s11243-007-0203-9openalex-snapshot
Activation of nitrite ion by biomimetic iron(III) complexes
inferred← citeshttps://doi.org/10.1007/s12274-022-4174-0openalex-snapshot
FeP nanorod array: A high-efficiency catalyst for electroreduction of NO to NH3 under ambient conditions
inferred← citeshttps://doi.org/10.1016/b0-08-043748-6/01066-5openalex-snapshot
Reactivity and Structure of Complexes of Small Molecules: Nitric and Nitrous Oxide
inferred← citeshttps://doi.org/10.1016/b0-08-043748-6/08172-xopenalex-snapshot
Electron Transfer: Cupredoxins
inferred← citeshttps://doi.org/10.1016/b978-0-08-102688-5.00111-2openalex-snapshot
Reactivity and Structure of Complexes of Small Molecules: Nitric Oxide
inferred← citeshttps://doi.org/10.1016/b978-0-08-102688-5.08172-1openalex-snapshot
Classic Perspectives - Electron Transfer: Cupredoxins
inferred← citeshttps://doi.org/10.1016/b978-0-12-396462-5.00004-0openalex-snapshot
Azanone (HNO) interaction with Hemeproteins and metalloporphyrins
inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.11678-6openalex-snapshot
The Biocoordination Chemistry of Nitric Oxide With Heme and Nonheme Iron Centers
inferred← citeshttps://doi.org/10.1016/b978-0-12-800934-5.00007-4openalex-snapshot
Non-Heme Transition Metal Complexes of HNO
inferred← citeshttps://doi.org/10.1016/b978-0-12-800934-5.00018-9openalex-snapshot
Is Azanone Endogenously Produced in Mammals?
inferred← citeshttps://doi.org/10.1016/b978-0-12-816491-4.00007-3openalex-snapshot
Enzyme-based electrochemical biosensors
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/b978-044452839-1.50017-6openalex-snapshot
Bioinorganic Chemistry of the HNO Ligand
inferred← citeshttps://doi.org/10.1016/bs.adioch.2014.10.001openalex-snapshot
Three Redox States of Metallonitrosyls in Aqueous Solution
inferred← citeshttps://doi.org/10.1016/bs.adioch.2014.11.003openalex-snapshot
NOx Linkage Isomerization in Metal Complexes
inferred← citeshttps://doi.org/10.1016/bs.adioch.2025.09.012openalex-snapshot
NO Linkage Isomerization in Metal Complexes
inferred← citeshttps://doi.org/10.1016/j.abb.2008.09.001openalex-snapshot
Spectroscopic and kinetic studies of Nor1, a cytochrome P450 nitric oxide reductase from the fungal pathogen Histoplasma capsulatum
inferred← citeshttps://doi.org/10.1016/j.bbabio.2010.10.020openalex-snapshot
The cytochrome c8 involved in the nitrite reduction pathway acts also as electron donor to the photosynthetic reaction center in Rubrivivax gelatinosus
inferred← citeshttps://doi.org/10.1016/j.bbabio.2013.03.010openalex-snapshot
Multi-heme proteins: Nature's electronic multi-purpose tool
inferred← citeshttps://doi.org/10.1016/j.bbabio.2015.06.014openalex-snapshot
Structure and properties of the catalytic site of nitric oxide reductase at ambient temperature
inferred← citeshttps://doi.org/10.1016/j.bbabio.2016.04.279openalex-snapshot
Electron transfer and docking between cytochrome cd 1 nitrite reductase and different redox partners — A comparative study
inferred← citeshttps://doi.org/10.1016/j.bbabio.2019.07.011openalex-snapshot
Complexome analysis of the nitrite-dependent methanotroph Methylomirabilis lanthanidiphila
inferred← citeshttps://doi.org/10.1016/j.bbagen.2017.10.011openalex-snapshot
Study of the Cys-His bridge electron transfer pathway in a copper-containing nitrite reductase by site-directed mutagenesis, spectroscopic, and computational methods
inferred← citeshttps://doi.org/10.1016/j.bbapap.2013.02.038openalex-snapshot
Small ligand–globin interactions: Reviewing lessons derived from computer simulation
inferred← citeshttps://doi.org/10.1016/j.bioelechem.2006.03.030openalex-snapshot
Electrochemical characterization of biosensor based on nitrite reductase and methyl viologen co-immobilized glassy carbon electrode
inferred← citeshttps://doi.org/10.1016/j.biortech.2017.05.161openalex-snapshot
Biological nutrient removal and molecular biological characteristics in an anaerobic-multistage anaerobic/oxic (A-MAO) process to treat municipal wastewater
inferred← citeshttps://doi.org/10.1016/j.cbpa.2014.01.017openalex-snapshot
Model complexes of key intermediates in fungal cytochrome P450 nitric oxide reductase (P450nor)
inferred← citeshttps://doi.org/10.1016/j.ccr.2005.06.018openalex-snapshot
Metal compounds and small molecules activation – case studies
inferred← citeshttps://doi.org/10.1016/j.ccr.2007.04.012openalex-snapshot
New features in the redox coordination chemistry of metal nitrosyls {M–NO+; M–NO; M–NO−(HNO)}
inferred← citeshttps://doi.org/10.1016/j.ccr.2009.07.021openalex-snapshot
Mechanistic studies of nitrite reactions with metalloproteins and models relevant to mammalian physiology
inferred← citeshttps://doi.org/10.1016/j.ccr.2011.10.023openalex-snapshot
Reductive N–N coupling of NO molecules on transition metal complexes leading to N2O
inferred← citeshttps://doi.org/10.1016/j.ccr.2013.02.007openalex-snapshot
Designing functional metalloproteins: From structural to catalytic metal sites
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.cej.2013.06.074openalex-snapshot
Botanical biofiltration of indoor gaseous pollutants – A mini-review
inferred← citeshttps://doi.org/10.1016/j.cej.2023.146257openalex-snapshot
Extremely high selective Si1−xGex-film wet etchant generating highly dissolved oxygen via peracetic acid oxidant for lateral gate-all-around FETs with a logic node of less than 3-nm
inferred← citeshttps://doi.org/10.1016/j.chemosphere.2018.11.143openalex-snapshot
Oxidation and reduction of redox-sensitive elements in the presence of humic substances in subsurface environments: A review
inferred← citeshttps://doi.org/10.1016/j.chemosphere.2023.139776openalex-snapshot
Bioelectrochemical system for nitrogen removal: Fundamentals, current status, trends, and challenges
inferred← citeshttps://doi.org/10.1016/j.chemosphere.2023.140026openalex-snapshot
Electrochemically-mediated reactive separation of nitric oxide into nitrate using iron chelate
inferred← citeshttps://doi.org/10.1016/j.cocr.2026.100030openalex-snapshot
Potential-controlled nitric oxide oxidation at copper centers: Inner-sphere electron transfer triggered by hydroxide attack on Cu–NO adducts
inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2016.12.011openalex-snapshot
Comparative analysis of amino acid composition in the active site of nirk gene encoding copper-containing nitrite reductase (CuNiR) in bacterial spp.
inferred← citeshttps://doi.org/10.1016/j.cplett.2005.10.087openalex-snapshot
How is NO bound to reduced copper nitrite reductase? A DFT study
inferred← citeshttps://doi.org/10.1016/j.crci.2006.11.005openalex-snapshot
Bioinspired electrocatalytic reduction of nitric oxide by immobilized heme groups
inferred← citeshttps://doi.org/10.1016/j.electacta.2018.10.179openalex-snapshot
Proton-coupled reduction of an iron nitrosyl porphyrin in the protic ionic liquid nanodomain
inferred← citeshttps://doi.org/10.1016/j.envpol.2022.120295openalex-snapshot
Contribution of nitrous oxide to the carbon footprint of full-scale wastewater treatment plants and mitigation strategies- a critical review
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2005.10.010openalex-snapshot
Enzyme technology and biological remediation
inferred← citeshttps://doi.org/10.1016/j.geoderma.2022.116300openalex-snapshot
Natural formation of copper sulfide nanoparticles via microbially mediated organic sulfur mineralization in soil: Processes and mechanisms
inferred← citeshttps://doi.org/10.1016/j.ibiod.2015.03.013openalex-snapshot
Surface and bacterial reduction of nitrate at alkaline pH: Conditions comparable to a nuclear waste repository
inferred← citeshttps://doi.org/10.1016/j.ica.2011.06.052openalex-snapshot
Synthesis, characterization and protonation reaction of copper and palladium complexes bearing nitrite ligands in O,O-bidentate and N-monodentate bonding fashions
inferred← citeshttps://doi.org/10.1016/j.ica.2015.05.009openalex-snapshot
Synthesis, structure and properties of tris(1-ethyl-4-isopropyl-imidazolyl-κN)phosphine copper(II)
inferred← citeshttps://doi.org/10.1016/j.ica.2017.06.027openalex-snapshot
Nitrogen dioxide reactivity of a Nickel(II) complex of tetraazacyclotetradecane ligand
inferred← citeshttps://doi.org/10.1016/j.ica.2019.02.036openalex-snapshot
Arrangement of a NO ligand and the neighboring sulfur-containing species on a dinuclear ruthenium complex by ligand substitution and linkage isomerism of a dimethyl sulfoxide ligand
inferred← citeshttps://doi.org/10.1016/j.inoche.2020.108069openalex-snapshot
Response of inorganic Al12N12 nano-cage toward nitrosyl hydride: A computational study
inferred← citeshttps://doi.org/10.1016/j.isci.2025.114322openalex-snapshot
Genome-wide regulon of NtrC reveals genetic regulation under nitrogen limitation in Methylomonas sp. DH-1
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.110290openalex-snapshot
Structural basis of cuproenzyme nitrite reduction at the level of a single hydrogen atom
inferred← citeshttps://doi.org/10.1016/j.jcat.2021.03.028openalex-snapshot
Catalytic reduction of nitrate by an oxidorhenium (V) complex
inferred← citeshttps://doi.org/10.1016/j.jcat.2025.116526openalex-snapshot
Enzyme-like denitrification with an oxidorhenium(V) complex: reduction of nitrite to N2O
inferred← citeshttps://doi.org/10.1016/j.jechem.2024.04.040openalex-snapshot
Strategic regulation of nitrogen-containing intermediates for enhanced nitrate reduction over Co3O4/SiC catalyst having multiple active centers
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2004.04.005openalex-snapshot
A nitrosyl hydride complex of a heme model [Ru(ttp)(HNO)(1-MeIm)] (ttp=tetratolylporphyrinato dianion)
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2004.09.024openalex-snapshot
Nitric oxide reductases of prokaryotes with emphasis on the respiratory, heme?copper oxidase type
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2004.11.005openalex-snapshot
Coordination chemistry of the HNO ligand with hemes and synthetic coordination complexes
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2007.08.002openalex-snapshot
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2008.01.014openalex-snapshot
Nitric oxide activation and reduction by heme–copper oxidoreductases and nitric oxide reductase
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2008.01.024openalex-snapshot
Alkaline transition of pseudoazurin Met16X mutant proteins: Protein stability influenced by the substitution of Met16 in the second sphere coordination
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2009.09.024openalex-snapshot
Disproportionation of hydroxylamine by water-soluble iron(III) porphyrinate compounds
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2009.11.004openalex-snapshot
Non-covalent interactions in blue copper protein probed by Met16 mutation and electronic and resonance Raman spectroscopy of Achromobacter cycloclastes pseudoazurin
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.04.016openalex-snapshot
Overexpression, purification, and biochemical and spectroscopic characterization of copper-containing nitrite reductase from Sinorhizobium meliloti 2011. Study of the interaction of the catalytic copper center with nitrite and NO
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.05.013openalex-snapshot
Ambidentate H-bonding of NO and O2 in heme proteins
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.08.026openalex-snapshot
Synthesis, properties, and reactivity of a series of non-heme {FeNO}7/8 complexes: Implications for Fe-nitroxyl coordination
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.09.023openalex-snapshot
Computational investigations of HNO in biology
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.10.009openalex-snapshot
Reactivity of iron(II)-bound nitrosyl hydride (HNO, nitroxyl) in aqueous solution
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2017.01.006openalex-snapshot
Heterologous expression of Halomonas halodenitrificans nitric oxide reductase and its N-terminally truncated NorC subunit in Escherichia coli
inferred← citeshttps://doi.org/10.1016/j.jmgm.2006.02.003openalex-snapshot
Binding mode analysis of the NADH cofactor in nitric oxide reductase: A theoretical study
inferred← citeshttps://doi.org/10.1016/j.mattod.2025.02.012openalex-snapshot
Boosting ammonia electrosynthesis via interfacial tandem nitrate reduction enabled by an amorphous@crystalline electrocatalyst
inferred← citeshttps://doi.org/10.1016/j.molstruc.2025.141723openalex-snapshot
Synthesis, crystal structure and antibacterial activity of diaqua sulfato 2,4,6-tris(2-pyridyl)-s-triazine Zn(II) dihydrate
inferred← citeshttps://doi.org/10.1016/j.niox.2005.03.006openalex-snapshot
Further evidence supporting an inner sphere mechanism in the NO reduction of the copper(II) complex Cu(dmp)22+ (dmp=2,9-dimethyl-1,10-phenanthroline)
inferred← citeshttps://doi.org/10.1016/j.niox.2012.09.003openalex-snapshot
Characterization of novel nitrite-based nitric oxide generating delivery systems for topical dermal application
inferred← citeshttps://doi.org/10.1016/j.niox.2013.10.004openalex-snapshot
Redox-mediated mechanisms and biological responses of copper-catalyzed reduction of the nitrite ion in vitro
inferred← citeshttps://doi.org/10.1016/j.poly.2003.09.036openalex-snapshot
A structural model for oxidized type II copper nitrite reductase with a polyimidazole tripodal ligand
inferred← citeshttps://doi.org/10.1016/j.poly.2007.03.048openalex-snapshot
Structural and physical characterization of (nitrato)iron(III) porphyrinates [Fe(por)(NO3)] – Variable coordination of nitrate
inferred← citeshttps://doi.org/10.1016/j.poly.2015.01.044openalex-snapshot
Molecular structure and nitrite-bonded study on copper(II) complexes of N,N-dialkyl,N′-benzyl-ethylenediamine; synthesis, spectroscopic characterization, X-ray structure, steric effect and density functional theory calculations
inferred← citeshttps://doi.org/10.1016/j.soilbio.2011.06.014openalex-snapshot
Formation of hybrid N2O and hybrid N2 due to codenitrification: First review of a barely considered process of microbially mediated N-nitrosation
inferred← citeshttps://doi.org/10.1016/j.soilbio.2014.09.025openalex-snapshot
A review of soil NO transformation: Associated processes and possible physiological significance on organisms
inferred← citeshttps://doi.org/10.1016/j.tetlet.2003.10.218openalex-snapshot
Pronounced stabilisation of the ferrocenium state of ferrocenecarboxylic acid by salt bridge formation with a benzamidine
inferred← citeshttps://doi.org/10.1016/j.theochem.2005.06.040openalex-snapshot
Hartree–Fock and density functional theory calculations for the reaction mechanism of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum
inferred← citeshttps://doi.org/10.1016/j.tifs.2026.105920openalex-snapshot
Nitrite reductases: From structure–function relationships to biocatalytic nitrite depletion and detection
inferred← citeshttps://doi.org/10.1016/j.ymeth.2013.04.016openalex-snapshot
Methods for detection and characterization of protein S-nitrosylation
inferred← citeshttps://doi.org/10.1016/s0005-2728(99)00017-1openalex-snapshot
Bacterial nitric oxide synthesis
inferred← citeshttps://doi.org/10.1016/s0005-2728(99)00021-3openalex-snapshot
Nitric oxide and iron proteins
inferred← citeshttps://doi.org/10.1016/s0005-2728(99)00032-8openalex-snapshot
Nitric oxide in bacteria: synthesis and consumption
inferred← citeshttps://doi.org/10.1016/s0010-8545(01)00472-6openalex-snapshot
To be or not to be NO in coordination chemistry? A mechanistic approach
inferred← citeshttps://doi.org/10.1016/s0010-8545(98)00254-9openalex-snapshot
Physical properties and mechanisms of formation of nitrous oxide
inferred← citeshttps://doi.org/10.1016/s0010-8545(99)00069-7openalex-snapshot
Structure–function relationships of copper-containing nitrite reductases
inferred← citeshttps://doi.org/10.1016/s0010-8545(99)00143-5openalex-snapshot
The chemical reduction of nitrate in aqueous solution
inferred← citeshttps://doi.org/10.1016/s0020-1693(00)00271-1openalex-snapshot
Copper complexes of a new tridentate imidazole-containing ligand: spectroscopy, structures and nitrite reductase reactivity
inferred← citeshttps://doi.org/10.1016/s0020-1693(02)00937-4openalex-snapshot
UV resonance Raman and NMR spectroscopic studies on the pH dependent metal ion release from pseudoazurin
inferred← citeshttps://doi.org/10.1016/s0020-1693(99)00404-1openalex-snapshot
Dioxygen and nitric oxide reactivity of a reduced heme/non-heme diiron(II) complex [(5L)FeII⋯FeIICl]+. Using a tethered tetraarylporphyrin for the development of an active site reactivity model for bacterial nitric oxide reductase
inferred← citeshttps://doi.org/10.1016/s0022-1139(00)00328-6openalex-snapshot
Fluorinated imidazoles as 19F probes for biomimetic studies of heme a3 — Cub site in cytochrome c oxidase
inferred← citeshttps://doi.org/10.1016/s0022-328x(02)01428-6openalex-snapshot
A comparative study on structures and theoretical models of Rh azido complexes
inferred← citeshttps://doi.org/10.1016/s0083-6729(05)72010-0openalex-snapshot
Nitric Oxide Signaling in Plants
inferred← citeshttps://doi.org/10.1016/s0162-0134(00)00174-4openalex-snapshot
Perturbations at the high spin heme b center in the membrane-bound nitric oxide reductase
inferred← citeshttps://doi.org/10.1016/s0166-526x(05)44010-6openalex-snapshot
Chapter 10 Non-affinity sensing technology: the exploitation of biocatalytic events for environmental analysis
inferred← citeshttps://doi.org/10.1016/s0277-5387(02)00872-0openalex-snapshot
Steric effects on the stereochemistry of copper complexes of 2,6-bis(pyrazol-1-ylmethyl)pyridines
inferred← citeshttps://doi.org/10.1016/s0378-1097(03)00821-8openalex-snapshot
Site-directed mutagenesis of NnrR: a transcriptional regulator of nitrite and nitric oxide reductase inRhodobacter sphaeroides
inferred← citeshttps://doi.org/10.1016/s0378-1097(98)00427-3openalex-snapshot
Denitrification by yeasts and occurrence of cytochrome P450nor in Trichosporon cutaneum
inferred← citeshttps://doi.org/10.1016/s0531-5131(02)00378-3openalex-snapshot
Cytochromes P450nor and P450foxy of the fungus Fusarium oxysporum
inferred← citeshttps://doi.org/10.1016/s0898-8838(00)51003-4openalex-snapshot
Structure and enzymology of two bacterial diheme enzymes: Cytochrome cd1 nitrite reductase and cytochrome c peroxidase
inferred← citeshttps://doi.org/10.1016/s0898-8838(03)54004-1openalex-snapshot
REACTION MECHANISMS OF NITRIC OXIDE WITH BIOLOGICALLY RELEVANT METAL CENTERS
inferred← citeshttps://doi.org/10.1016/s0898-8838(03)55002-4openalex-snapshot
REDOX REACTIVITY OF COORDINATED LIGANDS IN PENTACYANO(L)FERRATE COMPLEXES
inferred← citeshttps://doi.org/10.1016/s0898-8838(04)56006-3openalex-snapshot
TETRAPODAL PENTADENTATE NITROGEN LIGANDS: ASPECTS OF COMPLEX STRUCTURE AND REACTIVITY
inferred← citeshttps://doi.org/10.1016/s0969-2126(97)00267-0openalex-snapshot
N-terminal arm exchange is observed in the 2.15 Å crystal structure of oxidized nitrite reductase from Pseudomonas aeruginosa
inferred← citeshttps://doi.org/10.1016/s1046-5928(02)00575-2openalex-snapshot
Expression of recombinant Pseudomonas stutzeri di-heme cytochrome c4 by high-cell-density fed-batch cultivation of Pseudomonas putida
inferred← citeshttps://doi.org/10.1016/s1367-5931(98)80059-8openalex-snapshot
Nitrogen cycle enzymology
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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.