CaltechAUTHORS
Published August 2000 | Version public
Journal Article Metadata-only

Analyzing Your Complexes: Structure of the Quinol-Fumarate Reductase Respiratory Complex

Creators

  • 1. ROR icon California Institute of Technology
  • 2. ROR icon San Francisco VA Medical Center
  • 3. ROR icon University of California, San Francisco
  • 4. ROR icon University of California, Los Angeles
  • 5. ROR icon Howard Hughes Medical Institute

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.

Additional Information

© 2000 Elsevier Science Ltd. This work has been supported by the Department of Veterans Affairs (GC) and funding from the Howard Hughes Medical Institute (DCR), National Institutes of Health grants GM45162 (DCR) and HL-16251 (GC), and National Science Foundation grant MCB-9729778 (GC). We would like to acknowledge stimulating discussions with T Ohnishi, PL Dutton, HB Gray and S Iwata.

Additional details

Identifiers

Eprint ID
53414
Resolver ID
CaltechAUTHORS:20150108-154546091

Funding

Department of Veterans Affairs
Howard Hughes Medical Institute (HHMI)
NIH
GM45162
NIH
HL-16251
NSF
MCB-9729778

Dates

Created
2015-01-14
Created from EPrint's datestamp field
Updated
2021-11-10
Created from EPrint's last_modified field