The hows and whys of aerobic H-2 metabolism

Alison Parkin, Frank Sargent

    Research output: Contribution to journalReview articlepeer-review

    49 Citations (Scopus)


    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
    Issue number1-2
    Publication statusPublished - Apr 2012


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