Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum - Wikidata - awgldk - TriplyDB

Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum

Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum

http://www.wikidata.org/entity/Q27650029

about

Nitrate and periplasmic nitrate reductases The molybdenum oxotransferases and related enzymes.The mononuclear molybdenum enzymes.Molybdenum site structure of MOSC family proteins.Identification of Amino Acids at the Catalytic Site of a Ferredoxin-Dependent Cyanobacterial Nitrate Reductase Top-Down Characterization of the Post-Translationally Modified Intact Periplasmic Proteome from the Bacterium Novosphingobium aromaticivorans.Perchlorate Reductase Is Distinguished by Active Site Aromatic Gate Residues Roles of four conserved basic amino acids in a ferredoxin-dependent cyanobacterial nitrate reductase.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers Molybdenum and tungsten oxygen transferases--and functional diversity within a common active site motif.Structural and functional models in molybdenum and tungsten bioinorganic chemistry: description of selected model complexes, present scenario and possible future scopes.Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination.Nitrite reduction by molybdoenzymes: a new class of nitric oxide-forming nitrite reductases.Theoretical studies on mechanisms of some Mo enzymes.Structural and mechanistic insights on nitrate reductases.Bacterial molybdoenzymes: old enzymes for new purposes.A sulfurtransferase is essential for activity of formate dehydrogenases in Escherichia coli.Redundancy and modularity in membrane-associated dissimilatory nitrate reduction in Bacillus.Identification of the Ferredoxin-Binding Site of a Ferredoxin-Dependent Cyanobacterial Nitrate Reductase.Robust Production, Crystallization, Structure Determination, and Analysis of [Fe-S] Proteins: Uncovering Control of Electron Shuttling and Gating in the Respiratory Metabolism of Molybdopterin Guanine Dinucleotide Enzymes.Enzymatic “tricks”: Carboxylate shift and sulfur shift The Biosynthesis of the Molybdenum Cofactor in Escherichia coli and Its Connection to FeS Cluster Assembly and the Thiolation of tRNA

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P2860

Periplasmic nitrate reductase revisited: a sulfur atom completes the sixth coordination of the catalytic molybdenum

http://www.wikidata.org/entity/Q27650029

description

2008 nî lūn-bûn

@nan

2008 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի հունիսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

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S00775-008-0359-6

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Journal of Biological Inorganic Chemistry

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Periplasmic nitrate reductase ...... on of the catalytic molybdenum

@en

P2093

Abhik Mukhopadhyay

http://www.w3.org/2001/XMLSchema#string

Carlos C Romão

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Carlos D Brondino

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Catarina Coelho

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Isabel Moura

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José J G Moura

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José Trincão

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Maria J Romão

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Nuno M F S A Cerqueira

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Pablo J González

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P2860

Improved methods for building protein models in electron density maps and the location of errors in these models

A discussion of the solution for the best rotation to relate two sets of vectors

Bacterial respiration: a flexible process for a changing environment.

Equilibria amongst different molybdenum (V)-containing species from sulphite oxidase. Evidence for a halide ligand of molybdenum in the low-pH species.

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s00775-008-0359-6

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scholarly article

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10.1007/S00775-008-0359-6

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5

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13

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1049296456

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18327621

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