Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase

Curr Opin Struct Biol. 1999 Dec;9(6):663-9. doi: 10.1016/s0959-440x(99)00027-5.

Abstract

The first crystal structure of pyruvate:ferredoxin oxidoreductase to be determined has provided significant new information on its structural organization and redox chemistry. Spectroscopic analyses of a radical reaction intermediate have shed more light on its thiamin-based mechanism of catalysis. Different approaches have been used to study the interaction between the enzyme and ferredoxin, its redox partner.

Publication types

  • Review

MeSH terms

  • Electron Transport
  • Ketone Oxidoreductases / chemistry*
  • Ketone Oxidoreductases / metabolism*
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Pyruvate Synthase
  • Pyruvic Acid / metabolism
  • Thiamine Pyrophosphate / metabolism

Substances

  • Pyruvic Acid
  • Ketone Oxidoreductases
  • Pyruvate Synthase
  • Thiamine Pyrophosphate