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

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

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)7175-7178
Number of pages4
JournalChemical Communications
Early online date5 Jun 2018
Publication statusE-pub ahead of print - 5 Jun 2018

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.

Cite this