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How Escherichia coli is equipped to oxidize hydrogen under different redox conditions

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How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. / Lukey, M.J.; Parkin, A.; Roessler, M.M.; Murphy, B.J.; Harmer, J.; Armstrong, F.A. (Lead / Corresponding author); Palmer, T.; Sargent, F. (Lead / Corresponding author).

In: Journal of Biological Chemistry, Vol. 285, No. 6, 05.02.2010, p. 3928-3938.

Research output: Contribution to journalArticle

Harvard

Lukey, MJ, Parkin, A, Roessler, MM, Murphy, BJ, Harmer, J, Armstrong, FA, Palmer, T & Sargent, F 2010, 'How Escherichia coli is equipped to oxidize hydrogen under different redox conditions' Journal of Biological Chemistry, vol 285, no. 6, pp. 3928-3938.

APA

Lukey, M. J., Parkin, A., Roessler, M. M., Murphy, B. J., Harmer, J., Armstrong, F. A., Palmer, T., & Sargent, F. (2010). How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. Journal of Biological Chemistry, 285(6), 3928-3938doi: 10.1074/jbc.M109.067751, 10.1074/jbc.A109.067751

Vancouver

Lukey MJ, Parkin A, Roessler MM, Murphy BJ, Harmer J, Armstrong FA et al. How Escherichia coli is equipped to oxidize hydrogen under different redox conditions. Journal of Biological Chemistry. 2010 Feb 5;285(6):3928-3938.

Author

Lukey, M.J.; Parkin, A.; Roessler, M.M.; Murphy, B.J.; Harmer, J.; Armstrong, F.A. (Lead / Corresponding author); Palmer, T.; Sargent, F. (Lead / Corresponding author) / How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.

In: Journal of Biological Chemistry, Vol. 285, No. 6, 05.02.2010, p. 3928-3938.

Research output: Contribution to journalArticle

Bibtex - Download

@article{6f179696b6fb4f998a14ff5b7bc54963,
title = "How Escherichia coli is equipped to oxidize hydrogen under different redox conditions",
author = "M.J. Lukey and A. Parkin and M.M. Roessler and B.J. Murphy and J. Harmer and F.A. Armstrong and T. Palmer and F. Sargent",
note = "Erratum published June 25, 2010 The Journal of Biological Chemistry, 285, 20421",
year = "2010",
volume = "285",
number = "6",
pages = "3928--3938",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - How Escherichia coli is equipped to oxidize hydrogen under different redox conditions

A1 - Lukey,M.J.

A1 - Parkin,A.

A1 - Roessler,M.M.

A1 - Murphy,B.J.

A1 - Harmer,J.

A1 - Armstrong,F.A.

A1 - Palmer,T.

A1 - Sargent,F.

AU - Lukey,M.J.

AU - Parkin,A.

AU - Roessler,M.M.

AU - Murphy,B.J.

AU - Harmer,J.

AU - Armstrong,F.A.

AU - Palmer,T.

AU - Sargent,F.

PY - 2010/2/5

Y1 - 2010/2/5

N2 - The enterobacterium Escherichia coli synthesizes two H uptake enzymes, Hyd-1 and Hyd-2. We show using precise electrochemical kinetic measurements that the properties of Hyd-1 and Hyd-2 contrast strikingly, and may be individually optimized to function under distinct environmental conditions. Hyd-2 is well suited for fast and efficient catalysis in more reducing environments, to the extent that in vitro it behaves as a bidirectional hydrogenase. In contrast, Hyd-1 is active for H oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 isO tolerant and can oxidize H in the presence of air, whereas Hyd-2 is ineffective for H oxidation under aerobic conditions. The results have direct relevance for physiological roles of Hyd-1 and Hyd-2, which are expressed in different phases of growth. The properties that we report suggest distinct technological applications of these contrasting enzymes. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

AB - The enterobacterium Escherichia coli synthesizes two H uptake enzymes, Hyd-1 and Hyd-2. We show using precise electrochemical kinetic measurements that the properties of Hyd-1 and Hyd-2 contrast strikingly, and may be individually optimized to function under distinct environmental conditions. Hyd-2 is well suited for fast and efficient catalysis in more reducing environments, to the extent that in vitro it behaves as a bidirectional hydrogenase. In contrast, Hyd-1 is active for H oxidation under more oxidizing conditions and cannot function in reverse. Importantly, Hyd-1 isO tolerant and can oxidize H in the presence of air, whereas Hyd-2 is ineffective for H oxidation under aerobic conditions. The results have direct relevance for physiological roles of Hyd-1 and Hyd-2, which are expressed in different phases of growth. The properties that we report suggest distinct technological applications of these contrasting enzymes. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.

U2 - 10.1074/jbc.M109.067751

DO - 10.1074/jbc.M109.067751

M1 - Article

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 6

VL - 285

SP - 3928

EP - 3938

ER -

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