Journal
TOPICS IN CATALYSIS
Volume 58, Issue 12-13, Pages 699-707Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s11244-015-0412-y
Keywords
Hydrogenase; EPR spectroscopy; Radical SAM enzymes; Fe-S cluster enzymes
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Funding
- National Institute of General Medical Sciences of the National Institutes of Health [F32GM111025, GM104543]
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Proton reduction and H-2 oxidation are key elementary reactions for solar fuel production. Hydrogenases interconvert H+ and H-2 with remarkable efficiency and have therefore received much attention in this context. For [FeFe]-hydrogenases, catalysis occurs at a unique cofactor called the H-cluster. In this article, we discuss ways in which EPR spectroscopy has elucidated aspects of the bioassembly of the H-cluster, with a focus on four case studies: EPR spectroscopic identification of a radical en route to the CO and CN- ligands of the H-cluster, tracing Fe-57 from the maturase HydG into the H-cluster, characterization of the auxiliary Fe-S cluster in HydG, and isotopic labeling of the CN- ligands of HydA for electronic structure studies of its H-ox state. Advances in cell-free maturation protocols have enabled several of these mechanistic studies, and understanding H-cluster maturation may in turn provide insights leading to improvements in hydrogenase production for biotechnological applications.
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