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PMID: 11440857 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Large scale domain movement in cytochrome bc(1): a new device for electron transfer in proteins.

Trends in biochemical sciences ·Vol. 26 ·No. 7 ·2001-07-00 ·Pages 445-51

Darrouzet E, Moser CC, Dutton PL, Daldal F

Abstract

Recently, crystallographic, spectroscopic, kinetic and biochemical genetic data have merged to unveil a large domain movement for the Fe-S subunit in cytochrome bc(1). In this evolutionarily conserved enzyme, the domain motion acts to conduct intra-complex electron transfer and is essential for redox energy conversion.

MeSH Terms

Catalysis Electron Transport Electron Transport Complex III/chemistry Models, Chemical Models, Molecular Oxygen/chemistry Protein Structure, Tertiary Proteins/chemistry Thermodynamics

Chemicals

Proteins Electron Transport Complex III Oxygen

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Darrouzet E

Service de Biochimie Post-génomique et Toxicologie Nucléaire, DIEP, DSV, CEA VALRHO, 30207, Bagnols sur Cèze, France.

Moser C C

Dutton P L

Daldal F

Article Info

Journal

Trends in biochemical sciences

Abbr.

Trends Biochem Sci

ISSN

0968-0004

DOI

10.1016/s0968-0004(01)01897-7

Published

2001-07-00

Pages

445-51

Language

English

Region

England

NLM ID

7610674

Subset

Grants

NIGMS NIH HHS · R01 GM027309 · United States

NIGMS NIH HHS · R01 GM038237 · United States

NIGMS NIH HHS · GM 27309 · United States

NIGMS NIH HHS · GM 38237 · United States

External Links

PubMed source DOI: 10.1016/s0968-0004(01)01897-7 View journal details

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Large scale domain movement in cytochrome bc(1): a new device for electron transfer in proteins.

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