Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii

Chembiochem. 2015 Jul 27;16(11):1663-9. doi: 10.1002/cbic.201500130. Epub 2015 Jun 17.

Abstract

The transfer of photosynthetic electrons by the ferredoxin PetF to the [FeFe] hydrogenase HydA1 in the microalga Chlamydomonas reinhardtii is a key step in hydrogen production. Electron delivery requires a specific interaction between PetF and HydA1. However, because of the transient nature of the electron-transfer complex, a crystal structure remains elusive. Therefore, we performed protein-protein docking based on new experimental data from a solution NMR spectroscopy investigation of native and gallium-substituted PetF. This provides valuable information about residues crucial for complex formation and electron transfer. The derived complex model might help to pinpoint residue substitution targets for improved hydrogen production.

Keywords: NMR spectroscopy; electron transfer; hydrogenases; photosynthesis; protein-protein interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chlamydomonas reinhardtii / enzymology*
  • Ferredoxins / chemistry*
  • Ferredoxins / genetics
  • Ferredoxins / metabolism*
  • Gallium / chemistry
  • Hydrogen / metabolism
  • Hydrogenase / chemistry*
  • Hydrogenase / genetics
  • Hydrogenase / metabolism*
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular
  • Mutation
  • Oxidation-Reduction
  • Protein Binding
  • Protein Conformation

Substances

  • Ferredoxins
  • Hydrogen
  • Gallium
  • Hydrogenase