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Biochemistry ; 49(48): 10264-6, 2010 Dec 07.
Article in English | MEDLINE | ID: mdl-21058656

ABSTRACT

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.


Subject(s)
Hydrogen/metabolism , Hydrogenase/metabolism , Iron-Sulfur Proteins/metabolism , Light , Nanotechnology/methods , Nanowires/chemistry , Photosystem I Protein Complex/metabolism , Clostridium acetobutylicum/enzymology , Electron Transport/radiation effects , Hydrogenase/chemistry , Iron-Sulfur Proteins/chemistry , Models, Molecular , Photosystem I Protein Complex/chemistry , Protein Conformation
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