Biomimetic synthesis of a H2 catalyst using a protein cage architecture.
A biomimetic approach has been used to develop an artificial hydrogenase that catalyses the efficient reduction of protons producing hydrogen gas. Analogous to the unique biological metal clusters found in hydrogenase enzymes, the engineered active sites are small, well-defined Pt clusters deposited on the interior of a heat shock protein cage architecture with stoichiometries of 150 to 1000 Pt per protein cage. The proton reduction reaction is driven by visible light through a coupled reaction with Ru(bpy)3(2+) and methyl viologen as an electron-transfer mediator. Hydrogen production rates are comparable to those of hydrogenase on a per protein basis and exceed production rates of other reported Pt-based catalysts. These results demonstrate the utility of a biomimetic approach toward addressing the needs of hydrogen production.
Varpness
Z
Z
Department of Chemistry, Montana State University, Bozeman, Montana 59717, USA.
Peters
J W
JW
Young
M
M
Douglas
T
T
D019843:Archaeal Proteins / Q000737:chemistry; D002384:Catalysis; D006360:Heat-Shock Proteins / Q000737:chemistry; D006859:Hydrogen; D006864:Hydrogenase; D017017:Methanococcus / Q000737:chemistry; D008854:Microscopy, Electron; D008958:Models, Molecular; D018716:Molecular Mimicry; D049329:Nanostructures; D036103:Nanotechnology; D010984:Platinum; D011506:Proteins
D019843:Archaeal Proteins; D006360:Heat-Shock Proteins; D011506:Proteins; D010984:Platinum; D006859:Hydrogen; D006864:Hydrogenase