The hows and whys of aerobic H-2 metabolism

Alison Parkin; Frank Sargent

doi:10.1016/j.cbpa.2012.01.012

The hows and whys of aerobic H-2 metabolism

Alison Parkin, Frank Sargent

Research output: Contribution to journal › Review article › peer-review

56 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	26-34
Number of pages	9
Journal	Current Opinion in Chemical Biology
Volume	16
Issue number	1-2
DOIs	https://doi.org/10.1016/j.cbpa.2012.01.012
Publication status	Published - Apr 2012

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10.1016/j.cbpa.2012.01.012

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title = "The hows and whys of aerobic H-2 metabolism",

abstract = "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.",

author = "Alison Parkin and Frank Sargent",

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AU - Parkin, Alison

AU - Sargent, Frank

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N2 - 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.

AB - 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.

U2 - 10.1016/j.cbpa.2012.01.012

DO - 10.1016/j.cbpa.2012.01.012

M3 - Review article

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SP - 26

EP - 34

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

IS - 1-2

ER -

The hows and whys of aerobic H-2 metabolism

Abstract

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