Beyond H₂: exploiting 2-hydroxypyridine as a design element from [Fe]-hydrogenase for energy-relevant catalysis.

Cameron M Moore, Eric W Dahl, Nathaniel K Szymczak

Journal: Current opinion in chemical biology 2015;25():9-17

PMID: 25528204

Full Text on Elsevier Science View on PubMed

Abstract

The unique primary and secondary coordination environments surrounding the active site of hydrogenase enzymes play a crucial role in H2 activation and transfer reactions. [Fe]-hydrogenase contains a 2-hydroxypyridine ligand motif, and many researchers have incorporated this design element into synthetic catalysts. Transition metal complexes supported by 2-hydroxypyridine scaffolds are catalysts for chemical conversion schemes relevant to alternative energy applications and, in addition to hydrogenase-type reactivity, find new uses in other chemical domains. In this review, the current status of 2-hydroxypyridine-derived catalysts is described with an emphasis on design features that lead to lower energy catalytic pathways.

Address: Department of Chemistry, University of Michigan, 930 N. University Ave., Ann Arbor, MI 48109, United States.; Department of Chemistry, University of Michigan, 930 N. University Ave., Ann Arbor, MI 48109, United States. Electronic address: [email protected].

DOI: 10.1016/j.cbpa.2014.11.021

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MeSH Terms: Catalysis, Drug Design, Hydrogenase, Iron-Sulfur Proteins, Pyridones, Renewable Energy, Water