Evolution in the understanding of [Fe]-hydrogenase

Michael J Corr, John A Murphy

Research output: Contribution to journalArticle

48 Citations (Scopus)

Abstract

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.
LanguageEnglish
Pages2279-2292
Number of pages14
JournalChemical Society Reviews
Volume40
Issue number5
Early online date1 Mar 2011
DOIs
Publication statusPublished - 2011

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Hydrogenase
Hydrogen
Redox reactions
X ray crystallography
Reducing Agents
Methane
Enzymes
Nickel
Carbon Dioxide
Microorganisms
Iron
Metals
Economics
Substrates
iron hydrogenase

Keywords

  • chemical synthesis
  • enzyme type
  • hydrogenases
  • molecular hydrogen

Cite this

Corr, Michael J ; Murphy, John A. / Evolution in the understanding of [Fe]-hydrogenase. In: Chemical Society Reviews. 2011 ; Vol. 40, No. 5. pp. 2279-2292.
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Evolution in the understanding of [Fe]-hydrogenase. / Corr, Michael J; Murphy, John A.

In: Chemical Society Reviews, Vol. 40, No. 5, 2011, p. 2279-2292.

Research output: Contribution to journalArticle

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