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How Salmonella oxidises H-2 under aerobic conditions

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How Salmonella oxidises H-2 under aerobic conditions. / Parkin, Alison; Bowman, Lisa; Roessler, Maxie M.; Davies, Rosalind A.; Palmer, Tracy; Armstrong, Fraser A.; Sargent, Frank.

In: FEBS Letters, Vol. 586, No. 5, 2012, p. 536-544.

Research output: Contribution to journalArticle

Harvard

Parkin, A, Bowman, L, Roessler, MM, Davies, RA, Palmer, T, Armstrong, FA & Sargent, F 2012, 'How Salmonella oxidises H-2 under aerobic conditions' FEBS Letters, vol 586, no. 5, pp. 536-544., 10.1016/j.febslet.2011.07.044

APA

Parkin, A., Bowman, L., Roessler, M. M., Davies, R. A., Palmer, T., Armstrong, F. A., & Sargent, F. (2012). How Salmonella oxidises H-2 under aerobic conditions. FEBS Letters, 586(5), 536-544. 10.1016/j.febslet.2011.07.044

Vancouver

Parkin A, Bowman L, Roessler MM, Davies RA, Palmer T, Armstrong FA et al. How Salmonella oxidises H-2 under aerobic conditions. FEBS Letters. 2012;586(5):536-544. Available from: 10.1016/j.febslet.2011.07.044

Author

Parkin, Alison; Bowman, Lisa; Roessler, Maxie M.; Davies, Rosalind A.; Palmer, Tracy; Armstrong, Fraser A.; Sargent, Frank / How Salmonella oxidises H-2 under aerobic conditions.

In: FEBS Letters, Vol. 586, No. 5, 2012, p. 536-544.

Research output: Contribution to journalArticle

Bibtex - Download

@article{b6ff12929d2f4889890bcc642bae8410,
title = "How Salmonella oxidises H-2 under aerobic conditions",
author = "Alison Parkin and Lisa Bowman and Roessler, {Maxie M.} and Davies, {Rosalind A.} and Tracy Palmer and Armstrong, {Fraser A.} and Frank Sargent",
note = "Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.",
year = "2012",
doi = "10.1016/j.febslet.2011.07.044",
volume = "586",
number = "5",
pages = "536--544",
journal = "FEBS Letters",
issn = "0014-5793",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - How Salmonella oxidises H-2 under aerobic conditions

A1 - Parkin,Alison

A1 - Bowman,Lisa

A1 - Roessler,Maxie M.

A1 - Davies,Rosalind A.

A1 - Palmer,Tracy

A1 - Armstrong,Fraser A.

A1 - Sargent,Frank

AU - Parkin,Alison

AU - Bowman,Lisa

AU - Roessler,Maxie M.

AU - Davies,Rosalind A.

AU - Palmer,Tracy

AU - Armstrong,Fraser A.

AU - Sargent,Frank

PY - 2012

Y1 - 2012

N2 - <p>Salmonella enterica serovar Typhimurium is a Gram negative bacterial pathogen and a common cause of food-borne illness. Molecular hydrogen has been shown to be a key respiratory electron donor during infection and H-2 oxidation can be catalysed by three genetically-distinct [NiFe] hydrogenases. Of these, hydrogenases-1 (Hyd-1) and Hyd-2 have well-characterised homologues in Escherichia coli. The third, designated Hyd-5 here, is peculiar to Salmonella and is expressed under aerobic conditions. In this work, Salmonella was genetically modified to enable the isolation and characterisation of Hyd-5. Electrochemical analysis established that Hyd-5 is a H-2-oxidising enzyme that functions in very low levels of H-2 and sustains this activity in high levels of O-2. In addition, electron paramagnetic resonance spectroscopy of the Hyd-5 isoenzyme reveals a complex paramagnetic FeS signal at high potentials which is comparable to that observed for other O-2-tolerant respiratory [NiFe] hydrogenases. Taken altogether, Hyd-5 can be classified as an O-2-tolerant hydrogenase that confers upon Salmonella the ability to use H-2 as an electron donor in aerobic respiration. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.</p>

AB - <p>Salmonella enterica serovar Typhimurium is a Gram negative bacterial pathogen and a common cause of food-borne illness. Molecular hydrogen has been shown to be a key respiratory electron donor during infection and H-2 oxidation can be catalysed by three genetically-distinct [NiFe] hydrogenases. Of these, hydrogenases-1 (Hyd-1) and Hyd-2 have well-characterised homologues in Escherichia coli. The third, designated Hyd-5 here, is peculiar to Salmonella and is expressed under aerobic conditions. In this work, Salmonella was genetically modified to enable the isolation and characterisation of Hyd-5. Electrochemical analysis established that Hyd-5 is a H-2-oxidising enzyme that functions in very low levels of H-2 and sustains this activity in high levels of O-2. In addition, electron paramagnetic resonance spectroscopy of the Hyd-5 isoenzyme reveals a complex paramagnetic FeS signal at high potentials which is comparable to that observed for other O-2-tolerant respiratory [NiFe] hydrogenases. Taken altogether, Hyd-5 can be classified as an O-2-tolerant hydrogenase that confers upon Salmonella the ability to use H-2 as an electron donor in aerobic respiration. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.</p>

U2 - 10.1016/j.febslet.2011.07.044

DO - 10.1016/j.febslet.2011.07.044

M1 - Article

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 5

VL - 586

SP - 536

EP - 544

ER -

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