The hows and whys of aerobic H2 metabolism

Alison Parkin, Frank Sargent

Research output: Contribution to journalArticlepeer-review


The bacterial [NiFe]-hydrogenases have been classified as either 'standard' or 'O2-tolerant' based on their ability to function in the presence of O2. 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 O2 attack. In light of recent structural data and mutagenic studies this article reviews the molecular mechanism of O2-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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