title: Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii.
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.
authors.affiliation: Department for Biophysical Chemistry, Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany). wolfgang.lubitz@cec.mpg.de.
authors.forename: Sigrun
authors.initials: S
authors.lastname: Rumpel
authors.affiliation: Department for Biophysical Chemistry, Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany).
authors.forename: Judith F
authors.initials: JF
authors.lastname: Siebel
authors.affiliation: Department for Biophysical Chemistry, Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany).
authors.forename: Mamou
authors.initials: M
authors.lastname: Diallo
authors.affiliation: NMR Department, Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr (Germany).
authors.forename: Christophe
authors.initials: C
authors.lastname: Farès
authors.affiliation: Department for Biophysical Chemistry, Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany).
authors.forename: Edward J
authors.initials: EJ
authors.lastname: Reijerse
authors.affiliation: Department for Biophysical Chemistry, Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany). sigrun.rumpel@cec.mpg.de.
authors.forename: Wolfgang
authors.initials: W
authors.lastname: Lubitz
mesh_terms: D016825:Chlamydomonas reinhardtii / Q000201:enzymology*; D005288:Ferredoxins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D005708:Gallium / Q000737:chemistry; D006859:Hydrogen / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D009154:Mutation; D010084:Oxidation-Reduction; D011485:Protein Binding; D011487:Protein Conformation
chemical_list: D005288:Ferredoxins; D006859:Hydrogen; D005708:Gallium; D006864:Hydrogenase
keywords: NMR spectroscopy; electron transfer; hydrogenases; photosynthesis; protein-protein interactions