EPR Spectroscopic Studies of [FeFe]-Hydrogenase Maturation.
Proton reduction and H2oxidation are key elementary reactions for solar fuel production. Hydrogenases interconvert H+and H2with 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 radicalen routeto the CO and CN-ligands of the H-cluster, tracing57Fe 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 Hoxstate. 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.
Department of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
Daniel L M
DL
Suess
Department of Chemistry, University of California, One Shields Avenue, Davis, CA 95616, USA.
R David
RD
Britt
EPR spectroscopy; Fe–S cluster enzymes; Hydrogenase; Radical SAM enzymes