Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance

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Full text download(s)

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Published copy (DOI)

10.1039/C6CC00515B

Author(s)

Lindsey A Flanagan
John J Wright
Maxie M Roessler
James W Moir
Alison Parkin

Department/unit(s)

Publication details

Journal	Chemical Communications
Date	Accepted/In press - 31 Mar 2016
Date	E-pub ahead of print - 31 Mar 2016
Date	Published (current) - 12 Jul 2016
Issue number	58
Volume	52
Number of pages	4
Pages (from-to)	9133-6
Early online date	31/03/16
Original language	English

Abstract

Naturally occurring oxygen tolerant NiFe membrane bound hydrogenases have a conserved catalytic bias towards hydrogen oxidation which limits their technological value. We present an Escherichia coli Hyd-1 amino acid exchange that apparently causes the catalytic rate of H2 production to double but does not impact the O2 tolerance.

Bibliographical note

© The Royal Society of Chemistry 2016. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details

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Conserved Histidine Adjacent to the Proximal Cluster Tunes the Anaerobic Reductive Activation of Escherichia coli Membrane-Bound [NiFe] Hydrogenase-1

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