Chloroplast thioredoxin mutants without active-site cysteines facilitate the reduction of the regulatory disulphide bridge on the gamma-subunit of chloroplast ATP synthase.

Abstract excerpt

The activity of the chloroplast H+-ATPase (CFoCF1) is regulated by the proton electrochemical membrane potential and the reduction or the formation of the disulphide bridge on the gamma-subunit mediated by chloroplast thioredoxins (Trx). The latter regulation also applies to the water-soluble portion of CFoCF1 (CF1) and includes two successive steps, namely the binding of Trx to CF1 and the subsequent reduction...

Topics

• Binding Sites
• Chloroplast Thioredoxins
• Chloroplasts
• Cysteine
• Disulfides
• Dithiothreitol
• Enzyme Activation
• Models, Biological
• Mutation
• Oxidation-Reduction
• Protein Binding