In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer.

In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Research Abstract Details 

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In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Abstract Text:

Bettina Frangioni,Pascal Arnoux,Monique Sabaty,David Pignol,Patrick Bertrand,Bruno Guigliarelli,Christophe ,

The respiratory nitrate reductase (NapAB) from Rb. sphaeroides is a periplasmic molybdenum-containing enzyme which belongs to the DMSO reductase family. We report a study of NapAB by protein film voltammetry (PFV), and we present the first quantitative interpretation of the complex redox-state dependence of activity that has also been observed with other related enzymes. The model we use to fit the data assumes that binding of substrate partly limits turnover and is faster and weaker when the Mo ion is in the V oxidation state than when it is fully reduced. We explain how the presence in the catalytic cycle of such slow chemical steps coupled to electron transfer to the active site decreases the driving force required to reduce the MoV ion and makes exergonic the last intramolecular electron-transfer step (between the proximal cubane and the Mo cofactor). Importantly, comparison is made with all Mo enzymes for which PFV data are available, and we emphasize general features of the energetics of the catalytic cycles in enzymes of the DMSO reductase family.

In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Publishing Authors By Initials

B Frangioni,P Arnoux,M Sabaty,D Pignol,P Bertrand,B Guigliarelli,C ,

For similar bacteria: gram-negative bacteria: rhodobacter: rhodobacter sphaeroides research abstracts see: bacteria: gram-negative bacteria: rhodobacter: rhodobacter sphaeroides research

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In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of the American Chemical Society

VOLUME: 126

Page Numbers: 1328-9

Journal Abbreviation: J. Am. Chem. Soc.

ISSN: 0002-7863

DAY: 11

MONTH: Feb

YEAR: 2004

In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7503056

In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Keywords Mesh Terms:

KEYWORDS: Rhodobacter sphaeroides

MESH TERMS: enzymology

Chemical & Substance for Abstract: In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer. Information

Substance Name: Nitrate Reductase

Registry Number: EC 1.7.99.4

Grant and Affiliation Information for In Rhodobacter sphaeroides respiratory nitrate reductase, the kinetics of substrate binding favors intramolecular electron transfer.

AFFILIATION: Laboratoire de Bioénergétique et Ingénierie des Protéines, CNRS, 31 chemin J. Aiguier, 13402 Marseille, France.

Country: United States

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MEDLINETA: J Am Chem Soc

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