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X-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster

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Author(s)

  • Anne Volbeda
  • Jean-Marie Mouesca
  • Claudine Darnault
  • Maxie M. Roessler
  • Alison Parkin
  • Fraser A Armstrong
  • Juan C Fontecilla-Camps

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Publication details

JournalChemical communications
DateAccepted/In press - 4 Jun 2018
DateE-pub ahead of print (current) - 5 Jun 2018
Volume54
Number of pages4
Pages (from-to)7175-7178
Early online date5/06/18
Original languageEnglish

Abstract

The crystal structure of the Escherichia coli O2-sensitive C19G [NiFe]-hydrogenase-1 variant shows that the mutation results in a novel FeS cluster, proximal to the Ni–Fe active site. While the proximal cluster of the native O2-tolerant enzyme can transfer two electrons to that site, EPR spectroscopy shows that the modified cluster can transfer only one electron, this shortfall coinciding with O2 sensitivity. Computational studies on electron transfer help to explain how the structural and redox properties of the novel FeS cluster modulate the observed phenotype.

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© The Royal Society of Chemistry 2018. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details.

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