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Biomimetic Models of [FeFe]-hydrogenase: Utilization of peptides and redox non-innocent ligands in synthetic catalysts


Abstract [FeFe]-hydrogenases are enzymes for the reduction of protons to hydrogen. They rely on only the earth abundant first-row transition metal iron at their active site (H cluster). In recent years, a multitude of diiron mimics of hydrogenases have been synthesized, but none of them catalyzes hydrogen production with the same exquisite combination of high turnover frequency and low activation energy as the enzymes. Generally, model complexes fail to include one or both of two features essential to the natural enzyme: an intricate array of outer coordination sphere contacts that constrain the coordination geometry to attain a catalytically optimal conformation, and the redox non-innocence of accessory [FeS] clusters found at or near the hydrogen-... (more)
Created Date 2013
Contributor Roy, Souvik (Author) / Jones, Anne K (Advisor) / Moore, Thomas (Committee member) / Trovitch, Ryan (Committee member) / Arizona State University (Publisher)
Subject Chemistry
Type Doctoral Dissertation
Extent 213 pages
Language English
Copyright
Reuse Permissions All Rights Reserved
Note Ph.D. Chemistry 2013
Collaborating Institutions Graduate College / ASU Library
Additional Formats MODS / OAI Dublin Core / RIS


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Description Dissertation/Thesis