Display Settings:

Format

Send to:

Choose Destination
Biochim Biophys Acta. 2002 Jan 17;1553(1-2):102-16.

The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase.

Author information

  • 1Canadian Institutes of Health Research Group in the Molecular Biology of Membrane Proteins, Department of Biochemistry, University of Alberta, Edmonton, AB T6G 2H7, Canada. bernard.lemire@ualberta.ca

Abstract

The Saccharomyces cerevisiae succinate dehydrogenase (SDH) provides an excellent model system for studying the assembly, structure, and function of a mitochondrial succinate:quinone oxidoreductase. The powerful combination of genetic and biochemical approaches is better developed in yeast than in other eukaryotes. The yeast protein is strikingly similar to other family members in the structural and catalytic properties of its subunits. However, the membrane domain and particularly the role of the single heme in combination with two ubiquinone-binding sites need further investigation. The assembly of subunits and cofactors that occurs to produce new holoenzyme molecules is a complex process that relies on molecular chaperones. The yeast SDH provides the best opportunity for understanding the biogenesis of this family of iron-sulfur flavoproteins.

PMID:
11803020
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk