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Publication Abstract from PubMed

[NiFe] hydrogenases are complex model enzymes for the reversible cleavage of dihydrogen (H 2 ). However, structural determinants of efficient H 2 binding to their [NiFe] active site are not properly understood. Here, we present crystallographic and vibrational spectroscopic insights into the unexplored structure of the H 2 -binding [NiFe] intermediate. Using an F 420 -reducing [NiFe]-hydrogenase from Methanosarcina barkeri as a model enzyme, we show that the protein backbone provides a strained chelating scaffold that tunes the [NiFe] active site for efficient H 2 binding and conversion. The protein matrix also directs H 2 diffusion to the [NiFe] site via two gas channels and allows the distribution of electrons between functional protomers through a subunit-bridging FeS cluster. Our findings emphasize the relevance of an atypical Ni coordination, thereby providing a blueprint for the design of bio-inspired H 2 conversion catalysts.

X-ray Crystallography and Vibrational Spectroscopy Reveal Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] hydrogenases.,Ilina Y, Lorent C, Katz S, Jeoung JH, Shima S, Horch M, Zebger I, Dobbek H Angew Chem Int Ed Engl. 2019 Oct 7. doi: 10.1002/anie.201908258. PMID:31591784^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.