Progress in understanding structure-function relationships in respiratory chain complex II

FEBS Lett. 2000 Jan 21;466(1):1-5. doi: 10.1016/s0014-5793(99)01749-4.

Abstract

Complex II (succinate:quinone oxidoreductase) of aerobic respiratory chains oxidizes succinate to fumarate and passes the electrons directly into the quinone pool. It serves as the only direct link between activity in the citric acid cycle and electron transport in the membrane. Finer details of these reactions and interactions are but poorly understood. However, complex II has extremely similar structural and catalytic properties to quinol:fumarate oxidoreductases of anaerobic organisms, for which X-ray structures have recently become available. These offer new insights into structure-function relationships of this class of flavoenzymes, including evidence favoring protein movement during catalysis.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Catalysis
  • Electron Transport
  • Electron Transport Complex II
  • Escherichia coli / enzymology
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / metabolism
  • Models, Molecular
  • Multienzyme Complexes / chemistry*
  • Multienzyme Complexes / metabolism*
  • Oxidoreductases / chemistry*
  • Oxidoreductases / metabolism*
  • Protein Conformation
  • Protein Structure, Quaternary
  • Protein Structure, Secondary
  • Succinate Dehydrogenase / chemistry*
  • Succinate Dehydrogenase / metabolism*
  • Wolinella / enzymology

Substances

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