3 years ago

Reduction of the Catalytic [4Fe-4S] Cluster in [FeFe]-hydrogenases is coupled to Proton Transfer

Moritz Senger, Sven Timo Stripp, Ulf-Peter Apfel, Thomas Happe, Konstantin Laun, Florian Wittkamp, Jifu Duan, Martin Winkler, Michael Haumann
[FeFe]-hydrogenases catalyze the uptake and release of molecular hydrogen (H2) at a unique iron-sulfur cofactor. The absence of electrochemical overpotential in the H2 release reaction makes [FeFe]-hydrogenases a prime example of efficient biocatalysis. However, the molecular proceedings of hydrogen turnover are not understood yet. In this study, we characterize the initial one-electron reduction of [FeFe]-hydrogenases by infrared spectro-electrochemistry and present evidence for proton-coupled electron transport in the formation of the reduced state Hred´. Charge compensation stabilizes the excess electron at the [4Fe-4S] cluster and maintains a conservative configuration of the diiron site. The role of Hred´ in hydrogen turnover and possible implications on the catalytic mechanism are discussed. We suggest that the regulation of electronic properties in the periphery of metal cofactors is key to orchestrate multi-electron processes.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/anie.201709910

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