Wiring an [FeFe]-Hydrogenase with Photosystem I for Light-Induced Hydrogen Production

Tipo de material: Texto

TextoSeries ; BioChemistry, 49(48), p.10264-10266, 2010Trabajos contenidos:

Lubner Ce
Knorzer P
Silva Pj
Vincent Ka
Happe T
Bryant Da
Golbeck Jh

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Resumen: 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 (H2ase)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 FB iron-sulfur cluster of PS I and the distal iron-sulfur cluster of H2ase, 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 H2ase variant, and the molecular wire are combined.

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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 (H2ase)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 FB iron-sulfur cluster of PS I and the distal iron-sulfur cluster of H2ase, 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 H2ase variant, and the molecular wire are combined.

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