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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, 08:20 and posted on 22.02.2019, 17:02 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 Universit├Ąt Berlin

Country

Germany

ORCID For Submitting Author

0000-0002-8412-0258

Declaration of Conflict of Interest

No conflict of interest

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