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

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Farès,  Christophe
Service Department Farès (NMR), Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Citation

Rumpel, S., Siebel, J. F., Diallo, M., Farès, C., Reijerse, E. J., & Lubitz, W. (2015). Structural Insight into the Complex of Ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii. ChemBioChem: A European Journal of Chemical Biology, 16(11), 1663-1669. doi:10.1002/cbic.201500130.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0029-186D-E
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.