Hybrid metalloproteins incorporating synthetic organometallic active sites within a protein scaffold are being researched as viable catalysts for the production of hydrogen fuel. Our group and others have shown that the incorporation of cobalt protoporphyrin IX in cytochrome b₅₆₂ yields artificial enzymes that reduce protons to molecular hydrogen in the presence of photoinductive light and photosensitizers. Using random mutagenesis via error-prone PCR we have created a library of mutants to use in directed evolution to optimize hydrogen catalysis, though a challenge in this project is that testing individual variants by gas chromatography is not feasible on a large scale. For this reason, we are developing a gasochromic, hydrogen assay that is based on the interaction of molecular hydrogen with tungsten trioxide with a palladium catalyst. Initially, results show this assay to be qualitatively accurate between trials; however, its application in screening remains a challenge.
Details
- Tungsten Palladium Plates for Assaying H2 Catalysis by Cyt b562-CoPPIX
- Gutierrez, Elijah (Author)
- Ghirlanda, Giovana (Thesis director)
- Mills, Jeremy (Committee member)
- Redding, Kevin (Committee member)
- Barrett, The Honors College (Contributor)
- School of Molecular Sciences (Contributor)