Wiring an [FeFe]-hydrogenase with photosystem I for light-induced hydrogen production.
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.
Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.
Carolyn E
CE
Lubner
Philipp
P
Knörzer
Paulo J N
PJ
Silva
Kylie A
KA
Vincent
Thomas
T
Happe
Donald A
DA
Bryant
John H
JH
Golbeck
D046969:Clostridium acetobutylicum / Q000201:enzymology; D004579:Electron Transport / Q000528:radiation effects; D006859:Hydrogen / Q000378:metabolism*; D006864:Hydrogenase / Q000737:chemistry / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism*; D008027:Light; D008958:Models, Molecular; D036103:Nanotechnology / Q000379:methods*; D053770:Nanowires / Q000737:chemistry*; D045331:Photosystem I Protein Complex / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation
D007506:Iron-Sulfur Proteins; D045331:Photosystem I Protein Complex; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase