Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme.
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Protein design: toward functional metalloenzymesMolecular dynamics simulations reveal proton transfer pathways in cytochrome C-dependent nitric oxide reductaseRoles of glutamates and metal ions in a rationally designed nitric oxide reductase based on myoglobinIntroducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase ActivityDistinct roles of a tyrosine-associated hydrogen-bond network in fine-tuning the structure and function of heme proteins: two cases designed for myoglobinCharacterization of the nitric oxide reductase from Thermus thermophilus.Bioinspired heme, heme/nonheme diiron, heme/copper, and inorganic NOx chemistry: *NO((g)) oxidation, peroxynitrite-metal chemistry, and *NO((g)) reductive coupling.NO reduction by nitric-oxide reductase from denitrifying bacterium Pseudomonas aeruginosa: characterization of reaction intermediates that appear in the single turnover cycle.Spectroscopic characterization of heme iron-nitrosyl species and their role in NO reductase mechanisms in diiron proteins.Low-spin heme b(3) in the catalytic center of nitric oxide reductase from Pseudomonas nautica.Nitric oxide reductase (norB) genes from pure cultures and environmental samples.Investigating the Proton Donor in the NO Reductase from Paracoccus denitrificans.Functional importance of a pair of conserved glutamic acid residues and of Ca(2+) binding in the cbb(3)-type oxygen reductases from Rhodobacter sphaeroides and Vibrio cholerae.Recent advances in biosynthetic modeling of nitric oxide reductases and insights gained from nuclear resonance vibrational and other spectroscopic studies.O2 reduction by a functional heme/nonheme bis-iron NOR model complex.One heme, diverse functions: using biosynthetic myoglobin models to gain insights into heme-copper oxidases and nitric oxide reductases.Design of Heteronuclear Metalloenzymes.Bacterial adaptation of respiration from oxic to microoxic and anoxic conditions: redox control.Rational heme protein design: all roads lead to Rome.Why copper is preferred over iron for oxygen activation and reduction in haem-copper oxidases.Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities.A new assay for nitric oxide reductase reveals two conserved glutamate residues form the entrance to a proton-conducting channel in the bacterial enzyme.Active-site models of bacterial nitric oxide reductase featuring tris-histidyl and glutamic acid mimics: influence of a carboxylate ligand on Fe(B) binding and the heme Fe/Fe(B) redox potentialSubstrate control of internal electron transfer in bacterial nitric-oxide reductase.Structural basis for nitrous oxide generation by bacterial nitric oxide reductases.Efficient synthesis of trisimidazole and glutaric acid bearing porphyrins: ligands for active-site models of bacterial nitric oxide reductase.The nitric-oxide reductase from Paracoccus denitrificans uses a single specific proton pathway.Spectral properties of bacterial nitric-oxide reductase: resolution of pH-dependent forms of the active site heme b3.Defining the proton entry point in the bacterial respiratory nitric-oxide reductase.Redox-dependent open and closed forms of the active site of the bacterial respiratory nitric-oxide reductase revealed by cyanide binding studies.Experimental evidence for plasmid-borne nor-nir genes in Sinorhizobium meliloti JJ1c10.The impact of copper, nitrate and carbon status on the emission of nitrous oxide by two species of bacteria with biochemically distinct denitrification pathways.Characterization of the quinol-dependent nitric oxide reductase from the pathogen Neisseria meningitidis, an electrogenic enzyme.Unexpected weak magnetic exchange coupling between haem and non-haem iron in the catalytic site of nitric oxide reductase (NorBC) from Paracoccus denitrificans1.
P2860
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P2860
Two conserved glutamates in the bacterial nitric oxide reductase are essential for activity but not assembly of the enzyme.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
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2001年学术文章
@zh-my
2001年学术文章
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name
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@en
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@nl
type
label
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@en
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@nl
prefLabel
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@en
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@nl
P2093
P2860
P1476
Two conserved glutamates in th ...... ut not assembly of the enzyme.
@en
P2093
Richardson DJ
Watmough NJ
P2860
P304
P356
10.1128/JB.183.1.189-199.2001
P407
P577
2001-01-01T00:00:00Z