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The Geometry of the Catalytic Active Site in [FeFe]-Hydrogenases is Determined by Hydrogen Bonding and Proton Transfer

preprint
submitted on 22.02.2019 and posted on 22.02.2019 by Jifu Duan, Stefan Mebs, Moritz Senger, Konstantin Laun, Florian Wittkamp, Joachim Heberle, Thomas Happe, Eckhard Hofmann, Ulf-Peter Apfel, Martin Winkler, Michael Haumann, Sven T. Stripp
The H2 conversion and CO inhibition reactivity of nine [FeFe]-hydrogenase constructs with semi-artificial cofactors was studied by in situ and time-resolved infrared spectroscopy, X-ray crystallography, and theoretical methods. Impaired hydrogen turnover and proton transfer as well as characteristic CO inhibition/ reactivation kinetics are assigned to varying degrees of hydrogen-bonding interactions at the active site. We show that the probability to adopt catalytic intermediates is modulated by intramolecular and protein-cofactor interactions that govern structural dynamics at the active site of [FeFe]-hydrogenases.

History

Email Address of Submitting Author

sven.stripp@fu-berlin.de

Institution

Freie Universität Berlin

Country

Germany

ORCID For Submitting Author

0000-0002-8412-0258

Declaration of Conflict of Interest

No conflict of interest

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