Evolution in the understanding of [Fe]-hydrogenase

Michael J Corr, John A Murphy

Research output: Contribution to journalArticlepeer-review

56 Citations (Scopus)


Hydrogenases catalyse redox reactions with molecular hydrogen, either as substrate or product. The enzymes harness hydrogen as a reductant using metals that are abundant and economical, namely, nickel and iron, and should provide new pointers for the economic use of hydrogen in manmade devices. The most recently discovered and perhaps the most enigmatic of the hydrogenases is the [Fe]-hydrogenase, used by certain microorganisms in the pathway that reduces carbon dioxide to methane. Since its discovery some twenty years ago, [Fe]-hydrogenase has consistently provided structural and mechanistic surprises, often requiring complete re-evaluation of its mechanism of action. This tutorial review combines recent advances in X-ray crystallography and other analytical techniques, as well as in computational studies and in chemical synthesis to provide a platform for understanding this remarkable enzyme type.
Original languageEnglish
Pages (from-to)2279-2292
Number of pages14
JournalChemical Society Reviews
Issue number5
Early online date1 Mar 2011
Publication statusPublished - 2011


  • chemical synthesis
  • enzyme type
  • hydrogenases
  • molecular hydrogen


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