One of the greatest challenges facing society today is the development of a sustainable, carbon neutral energy source to curb the reliance on fossil fuel combustion as the primary source of energy. Research efforts have turned to biology for inspiration, as nature is adept at interconverting low molecular weight precursors into complex molecules. A number of inorganic catalysts have been reported for these conversions, however these inorganic models fail to achieve the high activity of enzymes as they lack critical protein secondary-shell interactions. To address these challenges, we have engineered two components of a bio-hybrid system in which protein scaffolds are used to modulate the properties of organometallic catalysts and inorganic clusters. We utilized a <i>de novo </i>designed peptide, the Domain Swapped Dimer (DSD), to bind both 3Fe4S and 4Fe4S clusters at discrete and tunable distances to function as an electron conduit. The synthesized peptides exhibit typical properties of iron-sulfur cluster proteins, are able to accept energy from an external photosensitizer, and can interface with natural redox proteins. The second component of the system utilizes cobalt protoporphyrin IX as an artificial catalyst. Mutagenesis in the primary and secondary shell of natural protein scaffolds is able to modulate proton-reduction activity by a factor of 5; the designed protein is able to function in aerobic conditions, a property unique to reductive catalysts. The designed system, produced from cheap precursors, offers the chance for scalable photocatalysis.

Design of protein-based hybrid catalysts for renewable fuel production

251st National Meeting (2016)

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