Biochemistry · 2010 · 123 citations · 17 references
Life SciencesBiochemistryChemistryCatalysisEnzymologyRedox BiochemistryElectron Transfer In ProteinsPhotocatalysisPhotochemistryPhotosynthetic Energy ConversionPhotosystem IRedox EnzymesDirect Electron TransferElectron TransferHydrogen GenerationIron-sulfur Cluster Electron TransferIron-sulfur Cluster Redox ChemistryPhotosystem I Electron TransferPhotosystem I Iron-sulfur ClustersPhotosystem I Redox Cofactors
A molecular wire is used to connect two proteins through their physiologically relevant redox cofactors to facilitate direct electron transfer. Photosystem I (PS I) and an [FeFe]-hydrogenase (H(2)ase) serve as the test bed for this new technology. By tethering a photosensitizer with a hydrogen-evolving catalyst, attached by Fe-S coordination bonds between the F(B) iron-sulfur cluster of PS I and the distal iron-sulfur cluster of H(2)ase, we assayed electron transfer between the two components via light-induced hydrogen generation. These hydrogen-producing nanoconstructs self-assemble when the PS I variant, the H(2)ase variant, and the molecular wire are combined.
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