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The hows and whys of aerobic H-2 metabolism

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The hows and whys of aerobic H-2 metabolism. / Parkin, Alison; Sargent, Frank.

In: Current Opinion in Chemical Biology, Vol. 16, No. 1-2, 04.2012, p. 26-34.

Research output: Contribution to journalScientific review

Harvard

Parkin, A & Sargent, F 2012, 'The hows and whys of aerobic H-2 metabolism' Current Opinion in Chemical Biology, vol 16, no. 1-2, pp. 26-34., 10.1016/j.cbpa.2012.01.012

APA

Parkin, A., & Sargent, F. (2012). The hows and whys of aerobic H-2 metabolism. Current Opinion in Chemical Biology, 16(1-2), 26-34. 10.1016/j.cbpa.2012.01.012

Vancouver

Parkin A, Sargent F. The hows and whys of aerobic H-2 metabolism. Current Opinion in Chemical Biology. 2012 Apr;16(1-2):26-34. Available from: 10.1016/j.cbpa.2012.01.012

Author

Parkin, Alison; Sargent, Frank / The hows and whys of aerobic H-2 metabolism.

In: Current Opinion in Chemical Biology, Vol. 16, No. 1-2, 04.2012, p. 26-34.

Research output: Contribution to journalScientific review

Bibtex - Download

@article{ea8db996ee6942d08c3702345cc67335,
title = "The hows and whys of aerobic H-2 metabolism",
author = "Alison Parkin and Frank Sargent",
year = "2012",
doi = "10.1016/j.cbpa.2012.01.012",
volume = "16",
number = "1-2",
pages = "26--34",
journal = "Current Opinion in Chemical Biology",
issn = "1367-5931",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - The hows and whys of aerobic H-2 metabolism

A1 - Parkin,Alison

A1 - Sargent,Frank

AU - Parkin,Alison

AU - Sargent,Frank

PY - 2012/4

Y1 - 2012/4

N2 - <p>The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O-2-tolerant' based on their ability to function in the presence of O-2. Typically, these enzymes contain four redox-active metal centers: a Ni-Fe-CO-2CN(-) active site and three electron-transferring Fe-S clusters. Recent research suggests that, rather than differences at the catalytic active site, it is a novel Fe-S cluster electron transfer (ET) relay that controls how [NiFe]-hydrogenases recover from O-2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O-2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.</p>

AB - <p>The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O-2-tolerant' based on their ability to function in the presence of O-2. Typically, these enzymes contain four redox-active metal centers: a Ni-Fe-CO-2CN(-) active site and three electron-transferring Fe-S clusters. Recent research suggests that, rather than differences at the catalytic active site, it is a novel Fe-S cluster electron transfer (ET) relay that controls how [NiFe]-hydrogenases recover from O-2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O-2-tolerance in [NiFe]-hydrogenases and discusses the biosynthesis of the unique Fe-S relay.</p>

U2 - 10.1016/j.cbpa.2012.01.012

DO - 10.1016/j.cbpa.2012.01.012

M1 - Scientific review

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

SN - 1367-5931

IS - 1-2

VL - 16

SP - 26

EP - 34

ER -

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