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Royal Society of Chemistry, Chemical Science, 32(14), p. 8531-8551, 2023

DOI: 10.1039/d2sc05641k

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Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase ‘Hyd-2’ from Escherichia coli

Journal article published in 2023 by Rhiannon M. Evans ORCID, Stephen E. Beaton, Patricia Rodriguez Macia ORCID, Yunjie Pang, Kin Long Wong ORCID, Leonie Kertess ORCID, William K. Myers ORCID, Ragnar Bjornsson ORCID, Philip A. Ash ORCID, Kylie A. Vincent ORCID, Stephen B. Carr ORCID, Fraser A. Armstrong ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

Changing the conserved active-site arginine of [NiFe]-hydrogenases into a lysine greatly lowers the rates of catalytic H2 activation in each direction and results in the extremely tight binding of a diatomic ligand.