2026-05-22T05:11:51Zhttps://keep.lib.asu.edu/oai/requestoai:keep.lib.asu.edu:node-1576432024-12-20T18:25:12Zoai_pmh:alloai_pmh:repo_items157643
https://hdl.handle.net/2286/R.I.54891
http://rightsstatements.org/vocab/InC/1.0/
2019
126 pages
Doctoral Dissertation
Academic theses
Text
eng
Bahrami Dizicheh, Zahra
Ghirlanda, Giovanna
Allen, James P.
Seo, Dong Kyun
Arizona State University
Doctoral Dissertation Chemistry 2019
Redox enzymes represent a big group of proteins and they serve as catalysts for<br/><br/>biological processes that involve electron transfer. These proteins contain a redox center<br/><br/>that determines their functional properties, and hence, altering this center or incorporating<br/><br/>non-biological redox cofactor to proteins has been used as a means to generate redox<br/><br/>proteins with desirable activities for biological and chemical applications. Porphyrins and<br/><br/>Fe-S clusters are among the most common cofactors that biology employs for electron<br/><br/>transfer processes and there have been many studies on potential activities that they offer<br/><br/>in redox reactions.<br/><br/>In this dissertation, redox activity of Fe-S clusters and catalytic activity of porphyrins<br/><br/>have been explored with regard to protein scaffolds. In the first part, modular property of<br/><br/>repeat proteins along with previously established protein design principles have been<br/><br/>used to incorporate multiple Fe-S clusters within the repeat protein scaffold. This study is<br/><br/>the first example of exploiting a single scaffold to assemble a determined number of<br/><br/>clusters. In exploring the catalytic activity of transmetallated porphyrins, a cobalt-porphyrin<br/><br/>binding protein known as cytochrome c was employed in a water oxidation<br/><br/>photoelectrochemical cell. This system can be further coupled to a hydrogen production<br/><br/>electrode to achieve a full water splitting tandem cell. Finally, a cobalt-porphyrin binding<br/><br/>protein known as cytochrome b562 was employed to design a whole cell catalysis system,<br/><br/>and the activity of the surface-displayed protein for hydrogen production was explored<br/><br/>photochemically. This system can further be expanded for directed evolution studies and<br/><br/>high-throughput screening.
Biochemistry
Chemistry, Inorganic
Biofuel
Catalysis
Cytochromes
Electron transfer
Iron-sulfur cluster
Porphyrins
Design of Redox Proteins as Catalysts for Fuel Production