By the same authors

From the same journal

From the same journal

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

Research output: Contribution to journalArticlepeer-review

Full text download(s)

Published copy (DOI)


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


Publication details

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


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.

Bibliographical note

© 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.

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations