Wiring an [FeFe]-hydrogenase with photosystem I for light-induced hydrogen production.

Journal article

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.

Authors: Lubner, C; Knörzer, P; Silva, P; Vincent, K; Happe, T

• Publication status: Published
• Journal: Biochemistry
• Volume: 49
• Issue: 48
• Pages: 10264-10266
• Publication date: 2010-12-01
• DOI: 10.1021/bi1016167
• EISSN: 1520-4995
• ISSN: 0006-2960
• Language: English
• Keywords: Clostridium acetobutylicum; Nanowires; Photosystem I Protein Complex; Iron-Sulfur Proteins; Electron Transport; Light; Protein Conformation; Hydrogenase; Models, Molecular; Hydrogen; Nanotechnology