One intriguing possibility for sustainable H2 production is the development of cellular systems in which light-driven oxygenic photosynthesis is efficiently coupled to hydrogen production by hydrogenase [Ihara et. al. Photochem. and Photobio. 2006]. For most hydrogenases, this reaction is highly sensitive to O2. One exception to this trend is the oxygen-tolerant membrane-bound [NiFe]-hydrogenase (MBH) from Ralstonia eutropha H16 [Goris et. al. Nature Chem. Bio. 2011]. It has recently been shown that electron throughput rates exceeding that of natural photosynthesis can be achieved using a biological/organic nanoconstruct [Lubner et. al. PNAS 2011]. However, the non-specific nature of this method results in the undesirable formulation of homodimers. We propose utilizing sortase-mediated ligation as a method for explicitly generating protein fusions between PSI of Synechoccus sp. PCC 6803 and the MBH of Ralstonia eutropha H16. The theory, strategy, and current progress of this work will be discussed.

Harnessing solar energy through enzyme mediated protein fusions

245th National Meeting (2013)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.