Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance

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 H(2) production to double but...

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Detalles Bibliográficos
Autores principales: Flanagan, Lindsey A., Wright, John J., Roessler, Maxie M., Moir, James W., Parkin, Alison
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Royal Society of Chemistry 2016
Materias:
Chemistry
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5040170/
https://www.ncbi.nlm.nih.gov/pubmed/27055899
http://dx.doi.org/10.1039/c6cc00515b
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author Flanagan, Lindsey A.
Wright, John J.
Roessler, Maxie M.
Moir, James W.
Parkin, Alison
author_facet Flanagan, Lindsey A.
Wright, John J.
Roessler, Maxie M.
Moir, James W.
Parkin, Alison
author_sort Flanagan, Lindsey A.
collection PubMed
description 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 H(2) production to double but does not impact the O(2) tolerance.
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spelling pubmed-50401702016-10-12 Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance Flanagan, Lindsey A. Wright, John J. Roessler, Maxie M. Moir, James W. Parkin, Alison Chem Commun (Camb) Chemistry 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 H(2) production to double but does not impact the O(2) tolerance. Royal Society of Chemistry 2016-07-25 2016-03-31 /pmc/articles/PMC5040170/ /pubmed/27055899 http://dx.doi.org/10.1039/c6cc00515b Text en This journal is © The Royal Society of Chemistry 2016 http://creativecommons.org/licenses/by/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution 3.0 Unported License (http://creativecommons.org/licenses/by/3.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Chemistry
Flanagan, Lindsey A.
Wright, John J.
Roessler, Maxie M.
Moir, James W.
Parkin, Alison
Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance
title Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance
title_full Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance
title_fullStr Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance
title_full_unstemmed Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance
title_short Re-engineering a NiFe hydrogenase to increase the H(2) production bias while maintaining native levels of O(2) tolerance
title_sort re-engineering a nife hydrogenase to increase the h(2) production bias while maintaining native levels of o(2) tolerance
topic Chemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5040170/
https://www.ncbi.nlm.nih.gov/pubmed/27055899
http://dx.doi.org/10.1039/c6cc00515b
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