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Analyzing your complexes: structure of the quinol-fumarate reductase respiratory complex
Author(s): Iverson TM, Luna-Chavez C, Schroder I, Cecchini G, Rees DC
Source: CURRENT OPINION IN STRUCTURAL BIOLOGY    Volume: 10    Issue: 4    Pages: 448-455    Published: AUG 2000  
Times Cited: 19     References: 55     
Abstract: The integral membrane protein complex quinol-fumarate reductase catalyzes the terminal step of a major anaerobic respiratory pathway. The homologous enzyme succinate-quinone oxidoreductase participates in aerobic respiration both as complex II and as a member of the Krebs cycle. Last year, two structures of quinol-fumarate reductases were reported. These structures revealed the cofactor organization linking the fumarate and quinol sites, and showed a cofactor arrangement across the membrane that is suggestive of a possible energy coupling function.
Document Type: Article
Language: English
Reprint Address: Iverson, TM (reprint author), CALTECH, 147-75 CH, Pasadena, CA 91125 USA
Addresses:
1. CALTECH, Pasadena, CA 91125 USA
2. Dept Vet Affairs Med Ctr, Div Mol Biol, San Francisco, CA 91421 USA
3. Univ Calif San Francisco, Dept Microbiol & Mol Genet, San Francisco, CA 94143 USA
4. Univ Calif Los Angeles, Dept Microbiol & Mol Genet, Los Angeles, CA 90095 USA
5. CALTECH, Howard Hughes Med Inst, Div Chem & Chem Engn, Pasadena, CA 91125 USA
Publisher: CURRENT BIOLOGY LTD, 84 THEOBALDS RD, LONDON WC1X 8RR, ENGLAND
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: 343CZ
ISSN: 0959-440X
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