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Structural and mechanistic insights on nitrate reductases
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Outgoing claims: the papers this work cites, builds on, or argues with.
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Evolution of Nitrate Reductase: Molecular and Structural Variations on a Common Function
inferredcites →https://doi.org/10.1002/jcc.21280openalex-snapshot
The effect of the sixth sulfur ligand in the catalytic mechanism of periplasmic nitrate reductase
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Enzymatic “tricks”: Carboxylate shift and sulfur shift
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Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution
inferredcites →https://doi.org/10.1007/pl00000845openalex-snapshot
Functional, biochemical and genetic diversity of prokaryotic nitrate reductases
inferredcites →https://doi.org/10.1007/pl00000846openalex-snapshot
The coordination and function of the redox centres of the membrane-bound nitrate reductases
inferredcites →https://doi.org/10.1007/s00775-008-0359-6openalex-snapshot
Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum
inferredcites →https://doi.org/10.1007/s00775-008-0416-1openalex-snapshot
Biochemical and spectroscopic characterization of the membrane-bound nitrate reductase from Marinobacter hydrocarbonoclasticus 617
inferredcites →https://doi.org/10.1007/s00775-009-0545-1openalex-snapshot
Density functional theory study of model complexes for the revised nitrate reductase active site in Desulfovibrio desulfuricans NapA
inferredcites →https://doi.org/10.1007/s00775-015-1237-7openalex-snapshot
Theoretical studies on mechanisms of some Mo enzymes
inferredcites →https://doi.org/10.1007/s007750100215openalex-snapshot
Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: metal identification and preliminary structural data by multi-wavelength crystallography
inferredcites →https://doi.org/10.1016/j.bbabio.2012.04.011openalex-snapshot
Substrate-dependent modulation of the enzymatic catalytic activity: Reduction of nitrate, chlorate and perchlorate by respiratory nitrate reductase from Marinobacter hydrocarbonoclasticus 617
inferredcites →https://doi.org/10.1016/j.bbabio.2013.01.011openalex-snapshot
The prokaryotic Mo/W-bisPGD enzymes family: A catalytic workhorse in bioenergetic
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Cell biology of molybdenum
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Molybdenum enzymes in higher organisms
inferredcites →https://doi.org/10.1016/j.ccr.2012.05.020openalex-snapshot
Periplasmic nitrate reductases and formate dehydrogenases: Biological control of the chemical properties of Mo and W for fine tuning of reactivity, substrate specificity and metabolic role
inferredcites →https://doi.org/10.1016/j.jmb.2011.03.016openalex-snapshot
The Crystal Structure of Cupriavidus necator Nitrate Reductase in Oxidized and Partially Reduced States
inferredcites →https://doi.org/10.1016/j.str.2003.11.020openalex-snapshot
Architecture of NarGH Reveals a Structural Classification of Mo-bisMGD Enzymes
inferredcites →https://doi.org/10.1016/s0969-2126(01)00566-4openalex-snapshot
Crystal Structure of the 100 kDa Arsenite Oxidase from Alcaligenes faecalis in Two Crystal Forms at 1.64 Å and 2.03 Å
inferredcites →https://doi.org/10.1016/s0969-2126(02)00826-2openalex-snapshot
Gene Sequence and the 1.8 Å Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio gigas
inferredcites →https://doi.org/10.1016/s0969-2126(99)80010-0openalex-snapshot
Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
inferredcites →https://doi.org/10.1021/bi002706bopenalex-snapshot
Catalytic Protein Film Voltammetry from a Respiratory Nitrate Reductase Provides Evidence for Complex Electrochemical Modulation of Enzyme Activity
inferredcites →https://doi.org/10.1021/bi012144bopenalex-snapshot
The 1.25 Å Resolution Structure of the Diheme NapB Subunit of Soluble Nitrate Reductase Reveals a Novel Cytochrome c Fold with a Stacked Heme Arrangement,
inferredcites →https://doi.org/10.1021/bi035869jopenalex-snapshot
Voltammetric Studies of the Catalytic Mechanism of the Respiratory Nitrate Reductase from Escherichia coli: How Nitrate Reduction and Inhibition Depend on the Oxidation State of the Active Site
inferredcites →https://doi.org/10.1021/bi952459popenalex-snapshot
Complete Coordination of the Four Fe-S Centers of the β Subunit from Escherichia coli Nitrate Reductase. Physiological, Biochemical, and EPR Characterization of Site-Directed Mutants Lacking the Highest or Lowest Potential [4Fe-4S] Clusters
inferredcites →https://doi.org/10.1021/bi972858fopenalex-snapshot
Molybdenum Cofactor Properties and [Fe-S] Cluster Coordination in Escherichia coli Nitrate Reductase A: Investigation by Site-Directed Mutagenesis of the Conserved His-50 Residue in the NarG Subunit
inferredcites →https://doi.org/10.1021/ic3028034openalex-snapshot
The Sulfur Shift: An Activation Mechanism for Periplasmic Nitrate Reductase and Formate Dehydrogenase
inferredcites →https://doi.org/10.1021/om9008197openalex-snapshot
Enzymatic Reduction of Nitrate to Nitrite: Insight from Density Functional Calculations
inferredcites →https://doi.org/10.1038/nature08302openalex-snapshot
Molybdenum cofactors, enzymes and pathways
inferredcites →https://doi.org/10.1038/nsb969openalex-snapshot
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
inferredcites →https://doi.org/10.1038/nsb994openalex-snapshot
Structural and redox plasticity in the heterodimeric periplasmic nitrate reductase
inferredcites →https://doi.org/10.1039/b821108fopenalex-snapshot
Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview
inferredcites →https://doi.org/10.1039/c3cs60249dopenalex-snapshot
Nitrate and periplasmic nitrate reductases
inferredcites →https://doi.org/10.1042/0264-6021:3560851openalex-snapshot
Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae
inferredcites →https://doi.org/10.1046/j.1365-2958.2002.02978.xopenalex-snapshot
Molecular analysis of dimethyl sulphide dehydrogenase from Rhodovulum sulfidophilum: its place in the dimethyl sulphoxide reductase family of microbial molybdopterin‐containing enzymes
inferredcites →https://doi.org/10.1074/jbc.m109.066027openalex-snapshot
Protein Crystallography Reveals a Role for the FS0 Cluster of Escherichia coli Nitrate Reductase A (NarGHI) in Enzyme Maturation
inferredcites →https://doi.org/10.1074/jbc.m410457200openalex-snapshot
Structural and Biochemical Characterization of a Quinol Binding Site of Escherichia coli Nitrate Reductase A
inferredcites →https://doi.org/10.1074/jbc.m607353200openalex-snapshot
Spectropotentiometric and Structural Analysis of the Periplasmic Nitrate Reductase from Escherichia coli
inferredcites →https://doi.org/10.1105/tpc.104.029694openalex-snapshot
Structural Basis of Eukaryotic Nitrate Reduction: Crystal Structures of the Nitrate Reductase Active Site
inferredcites →https://doi.org/10.1107/s0907444900018011openalex-snapshot
Crystallization and preliminary X-ray analysis of the recombinant dihaem cytochromec(NapB) fromHaemophilus influenzae
inferredcites →https://doi.org/10.1107/s0907444901017723openalex-snapshot
Purification and crystallization of the respiratory complex formate dehydrogenase-N fromEscherichia coli
inferredcites →https://doi.org/10.1126/science.272.5268.1615openalex-snapshot
Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
inferredcites →https://doi.org/10.1126/science.275.5304.1305openalex-snapshot
Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe 4 S 4 Cluster
inferredcites →https://doi.org/10.1201/9780203909331-12openalex-snapshot
Molybdenum Nitrogenases: A Crystallographic and Mechanistic View
inferredcites →https://doi.org/10.1201/9780203909331-15openalex-snapshot
Molybdenum Enzymes Containing the Pyranopterin Cofactor: An Overview
inferredcites →https://doi.org/10.1371/journal.pone.0072535openalex-snapshot
The Respiratory Arsenite Oxidase: Structure and the Role of Residues Surrounding the Rieske Cluster
inferredcites →https://doi.org/10.3109/07388554409079834openalex-snapshot
Biosynthesis of the Iron-Molybdenum Cofactor of Nitrogenase
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Vers une meilleure compréhension du mécanisme de transfert de soufre pour la maturation des formiate déshydrogénases microbiennes
inferred← citeshttps://doi.org/10.70675/8ab3e6dfzef19z48eezb4edz6121587decb6openalex-snapshot
Synthèse et rôle de l'oxyde nitrique d'origine bactérienne dans la symbiose fixatrice d'azote Ensifer meliloti-Medicago truncatula
inferred← citeshttps://doi.org/10.70675/98c97fb0z75d6z46a4zbca0z7899c40519edopenalex-snapshot
Investigation par spectroscopie RPE des bases moléculaires de la réactivité d'une enzyme à molybdène : la nitrate réductase périplasmique de Rhodobacter sphaeroides
inferred← citeshttps://doi.org/10.7150/jgen.28153openalex-snapshot
Genomic Insights Into A Novel, Alkalitolerant Nitrogen Fixing Bacteria, Azonexus sp. Strain ZS02
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