Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its 
Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate

Murphy, Bonnie J.; Hidalgo, Ricardo; Roessler, Maxie M.; Evans, Rhiannon, M.; Ash, Philip A.; Myers, William K.; Vincent, Kylie A.; Armstrong, Fraser A.

doi:10.1021/jacs.5b03182

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Discovery of Dark pH-Dependent H(⁺) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate

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Murphy, B. J., Hidalgo, R., Roessler, M. M., Evans, R. M., Ash, P. A., Myers, W. K., et al. (2015). Discovery of Dark pH-Dependent H(⁺) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate. Journal of the American Chemical Society, 137(26), 8484-8489. doi:10.1021/jacs.5b03182.

Cite as: http://hdl.handle.net/21.11116/0000-0006-A88D-E

Abstract

Despite extensive studies on [NiFe]-hydrogenases, the mechanism by which these enzymes produce and activate H₂ so efficiently remains unclear. A well-known EPR-active state produced under H₂ and known as Ni-C is assigned as a Ni^III-Fe^II species with a hydrido ligand in the bridging position between the two metals. It has long been known that low-temperature photolysis of Ni-C yields distinctive EPR-active states, collectively termed Ni-L, that are attributed to migration of the bridging-H species as a proton; however, Ni-L has mainly been regarded as an artifact with no mechanistic relevance. It is now demonstrated, based on EPR and infrared spectroscopic studies, that the Ni-C to Ni-L interconversion in Hydrogenase-1 (Hyd-1) from Escherichia coli is a pH-dependent process that proceeds readily in the dark-proton migration from Ni-C being favored as the pH is increased. The persistence of Ni-L in Hyd-1 must relate to unassigned differences in proton affinities of metal and adjacent amino acid sites, although the unusually high reduction potentials of the adjacent Fe-S centers in this O₂-tolerant hydrogenase might also be a contributory factor, impeding elementary electron transfer off the [NiFe] site after proton departure. The results provide compelling evidence that Ni-L is a true, albeit elusive, catalytic intermediate of [NiFe]-hydrogenases.