The Saccharomyces cerevisiae mitochondrial succinate:ubiquinone oxidoreductase

Biochim Biophys Acta. 2002 Jan 17;1553(1-2):102-16. doi: 10.1016/s0005-2728(01)00229-8.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Cell Membrane / chemistry
  • Cell Membrane / metabolism
  • Electron Transport Complex II
  • Flavoproteins / chemistry
  • Gene Expression Regulation, Enzymologic
  • Heme / chemistry
  • Iron-Sulfur Proteins / chemistry
  • Membrane Proteins / chemistry
  • Mitochondria / enzymology
  • Molecular Sequence Data
  • Multienzyme Complexes / metabolism*
  • Oxidoreductases / metabolism*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Succinate Dehydrogenase / chemistry
  • Succinate Dehydrogenase / genetics
  • Succinate Dehydrogenase / metabolism*


  • Flavoproteins
  • Iron-Sulfur Proteins
  • Membrane Proteins
  • Multienzyme Complexes
  • Heme
  • Oxidoreductases
  • Electron Transport Complex II
  • Succinate Dehydrogenase