Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities

scientific article published on 16 September 2016

Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/IJCH.201600033
P932PMC publication ID5161413
P698PubMed publication ID27994254

P50authorYi LuQ42588277
P2093author name stringAmbika Bhagi-Damodaran
Igor Petrik
P2860cites workGenome of the Epsilonproteobacterial Chemolithoautotroph Sulfurimonas denitrificansQ22065504
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The proton donor for O-O bond scission by cytochrome c oxidaseQ36825382
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Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzymeQ39501718
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Participation of nitric oxide reductase in survival of Pseudomonas aeruginosa in LPS-activated macrophages.Q40169951
Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo.Q40854863
A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme.Q41084853
Cytochrome bd terminal oxidaseQ41613753
Active site of cytochrome cbb3.Q41763465
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Redox-dependent structural changes in an engineered heme-copper center in myoglobin: insights into chloride binding to CuB in heme copper oxidasesQ46454406
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Role of heme types in heme-copper oxidases: effects of replacing a heme b with a heme o mimic in an engineered heme-copper center in myoglobinQ46817667
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Why is the reduction of NO in cytochrome c dependent nitric oxide reductase (cNOR) not electrogenic?Q51040816
Cytochrome c oxidase catalysis of the reduction of nitric oxide to nitrous oxide.Q51598904
The post-translational modification in cytochrome c oxidase is required to establish a functional environment of the catalytic site.Q52532194
The superfamily of heme-copper oxygen reductases: types and evolutionary considerations.Q53212737
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From Myoglobin to Heme-Copper Oxidase: Design and Engineering of a CuBCenter into Sperm Whale MyoglobinQ58032235
Cryoradiolysis as a Method for Mechanistic Studies in Inorganic BiochemistryQ58035694
Chloride Bound to Oxidized CytochromecOxidase Controls the Reaction with Nitric OxideQ58070481
Enzymatic versus Inorganic Oxygen Reduction Catalysts: Comparison of the Energy Levels in a Free-Energy SchemeQ63973892
Effects of buried ionizable amino acids on the reduction potential of recombinant myoglobinQ66778010
Spectroelectrochemical study of the cytochrome a site in carbon monoxide inhibited cytochrome c oxidaseQ70132265
[Optical and ESR-spectroscopic study of electronic adducts of oxymyoglobin and oxyhemoglobin]Q72848688
Purification and initial kinetic and spectroscopic characterization of NO reductase from Paracoccus denitrificansQ73066929
A low-redox potential heme in the dinuclear center of bacterial nitric oxide reductase: implications for the evolution of energy-conserving heme-copper oxidasesQ73101303
Resonance Raman, infrared, and EPR investigation on the binuclear site structure of the heme-copper ubiquinol oxidases from Acetobacter aceti: effect of the heme peripheral formyl group substitutionQ73800090
Heme/Copper Terminal OxidasesQ77646446
Dissimilatory Nitrite and Nitric Oxide ReductasesQ77646459
Accommodation of NO in the active site of mammalian and bacterial cytochrome c oxidase aa3Q80158971
P407language of work or nameEnglishQ1860
P304page(s)773-790
P577publication date2016-09-16
P1433published inIsrael Journal of ChemistryQ3155650
P1476titleUsing Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities
P478volume56

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cites work (P2860)
Q39030299Activation of dioxygen by copper metalloproteins and insights from model complexes.
Q48128628Bioinspired Synthesis of Cu2+ -Modified Covalent Triazine Framework: A New Highly Efficient and Promising Peroxidase Mimic
Q89932237Biological and Bioinspired Inorganic N-N Bond-Forming Reactions
Q48216892Copper(I)/NO(g) Reductive Coupling Producing a trans-Hyponitrite Bridged Dicopper(II) Complex: Redox Reversal Giving Copper(I)/NO(g) Disproportionation.
Q46342369Critical Aspects of Heme-Peroxo-Cu Complex Structure and Nature of Proton Source Dictate Metal-O(peroxo) Breakage versus Reductive O-O Cleavage Chemistry.
Q47902213Insights Into How Heme Reduction Potentials Modulate Enzymatic Activities of a Myoglobin-based Functional Oxidase
Q58101818Synthetic Fe/Cu Complexes: Toward Understanding Heme-Copper Oxidase Structure and Function

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