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From the same journal

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

Research output: Contribution to journalArticlepeer-review

Standard

Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance. / Flanagan, Lindsey A; Wright, John J; Roessler, Maxie M; Moir, James W; Parkin, Alison.

In: Chemical Communications, Vol. 52, No. 58, 12.07.2016, p. 9133-6.

Research output: Contribution to journalArticlepeer-review

Harvard

Flanagan, LA, Wright, JJ, Roessler, MM, Moir, JW & Parkin, A 2016, 'Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance', Chemical Communications, vol. 52, no. 58, pp. 9133-6. https://doi.org/10.1039/C6CC00515B

APA

Flanagan, L. A., Wright, J. J., Roessler, M. M., Moir, J. W., & Parkin, A. (2016). Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance. Chemical Communications, 52(58), 9133-6. https://doi.org/10.1039/C6CC00515B

Vancouver

Flanagan LA, Wright JJ, Roessler MM, Moir JW, Parkin A. Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance. Chemical Communications. 2016 Jul 12;52(58):9133-6. https://doi.org/10.1039/C6CC00515B

Author

Flanagan, Lindsey A ; Wright, John J ; Roessler, Maxie M ; Moir, James W ; Parkin, Alison. / Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance. In: Chemical Communications. 2016 ; Vol. 52, No. 58. pp. 9133-6.

Bibtex - Download

@article{e1893be96c08497584da67f55494d016,
title = "Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance",
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.",
author = "Flanagan, {Lindsey A} and Wright, {John J} and Roessler, {Maxie M} and Moir, {James W} and Alison Parkin",
note = "{\textcopyright} The Royal Society of Chemistry 2016. This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. Further copying may not be permitted; contact the publisher for details",
year = "2016",
month = jul,
day = "12",
doi = "10.1039/C6CC00515B",
language = "English",
volume = "52",
pages = "9133--6",
journal = "Chemical communications",
issn = "1359-7345",
publisher = "The Royal Society of Chemistry",
number = "58",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance

AU - Flanagan, Lindsey A

AU - Wright, John J

AU - Roessler, Maxie M

AU - Moir, James W

AU - Parkin, Alison

N1 - © 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

PY - 2016/7/12

Y1 - 2016/7/12

N2 - 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.

AB - 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.

U2 - 10.1039/C6CC00515B

DO - 10.1039/C6CC00515B

M3 - Article

C2 - 27055899

VL - 52

SP - 9133

EP - 9136

JO - Chemical communications

JF - Chemical communications

SN - 1359-7345

IS - 58

ER -