Hydrogen activation in nature is catalyzed by hydrogenases that utilize unique organometallic, transition metal centers caged in a protein that provides the coordination environment for fast proton and electron transfer. Hydrogenases possess many characteristics of an ideal catalyst, and elucidation of their basic structure-function properties are helping to guide efforts in development of synthetic catalysts for hydrogen production from water-splitting. In photosynthetic microbes hydrogenases catalyze the conversion of photoreductant from water-splitting into hydrogen. The conversion steps are mediated by formation of both stable and transient protein-protein complexes involving electrostatic interactions to orient donor-acceptor sites. The same principles have been used to guide the design and assembly of hydrogenase-nanoparticle hybrids for photocatalytic hydrogen production. Due to the sensitivity of nanoparticle relaxation kinetics to changes in charge-transfer pathways, spectroscopic and optical techniques can be used to probe the process of molecular assembly leading to formation of catalytic complexes. Our recent progress in the study of hydrogenases, and of hydrogenase-nanoparticle complexes will be presented and discussed.
ASJC Scopus subject areas
- Chemical Engineering(all)