The hows and whys of aerobic H-2 metabolism

Alison Parkin, Frank Sargent

    Research output: Contribution to journalReview article

    47 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 languageEnglish
    Pages (from-to)26-34
    Number of pages9
    JournalCurrent Opinion in Chemical Biology
    Volume16
    Issue number1-2
    DOIs
    Publication statusPublished - Apr 2012

    Cite this

    Parkin, Alison ; Sargent, Frank. / The hows and whys of aerobic H-2 metabolism. In: Current Opinion in Chemical Biology. 2012 ; Vol. 16, No. 1-2. pp. 26-34.
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    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.",
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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 journalReview article

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

    AU - Parkin, Alison

    AU - Sargent, Frank

    PY - 2012/4

    Y1 - 2012/4

    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

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    JO - Current Opinion in Chemical Biology

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