Redox signaling in chloroplasts: cleavage of disulfides by an iron-sulfur cluster

Science. 2000 Jan 28;287(5453):655-8. doi: 10.1126/science.287.5453.655.

Abstract

Light generates reducing equivalents in chloroplasts that are used not only for carbon reduction, but also for the regulation of the activity of chloroplast enzymes by reduction of regulatory disulfides via the ferredoxin:thioredoxin reductase (FTR) system. FTR, the key electron/thiol transducer enzyme in this pathway, is unique in that it can reduce disulfides by an iron-sulfur cluster, a property that is explained by the tight contact of its active-site disulfide and the iron-sulfur center. The thin, flat FTR molecule makes the two-electron reduction possible by forming on one side a mixed disulfide with thioredoxin and by providing on the opposite side access to ferredoxin for delivering electrons.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Catalytic Domain
  • Chloroplasts / metabolism*
  • Crystallography, X-Ray
  • Cyanobacteria / enzymology*
  • Cysteine / chemistry
  • Dimerization
  • Disulfides / chemistry
  • Disulfides / metabolism*
  • Electron Transport
  • Ferredoxins / metabolism
  • Hydrogen Bonding
  • Iron / chemistry
  • Iron-Sulfur Proteins
  • Models, Molecular
  • Oxidation-Reduction
  • Oxidoreductases / chemistry*
  • Oxidoreductases / metabolism*
  • Protein Structure, Secondary
  • Signal Transduction
  • Thioredoxins / metabolism

Substances

  • Disulfides
  • Ferredoxins
  • Iron-Sulfur Proteins
  • Thioredoxins
  • Iron
  • Oxidoreductases
  • ferredoxin-thioredoxin reductase
  • Cysteine

Associated data

  • PDB/1DJ7