Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydAΔEFG

David W. Mulder, Eric S. Boyd, Ranjana Sarma, Rachel K. Lange, James A. Endrizzi, Joan B. Broderick and John W. Peters ()
Additional contact information
David W. Mulder: Astrobiology Biogeocatalysis Research Center,
Eric S. Boyd: Astrobiology Biogeocatalysis Research Center,
Ranjana Sarma: Astrobiology Biogeocatalysis Research Center,
Rachel K. Lange: Astrobiology Biogeocatalysis Research Center,
James A. Endrizzi: Astrobiology Biogeocatalysis Research Center,
Joan B. Broderick: Astrobiology Biogeocatalysis Research Center,
John W. Peters: Astrobiology Biogeocatalysis Research Center,

Nature, 2010, vol. 465, issue 7295, 248-251

Abstract: Complex metalloenzyme structures Hydrogen metabolism is facilitated by the activity of three metalloenzymes: the [NiFe]- and [FeFe]-hydrogenases and the Hmd or [Fe]-hydrogenases. The catalytic core of the [FeFe]-hydrogenase (HydA) exists as a [4Fe–4S] cluster linked to a modified 2Fe subcluster. In this paper, Mulder et al. solved the X-ray crystal structure of HydA expressed in a genetic background that did not contain three other hydrogenase biosynthetic genes — the structure reveals a [4Fe–4S] cluster and an open pocket for the 2Fe subcluster. This means that H-cluster synthesis occurs in a stepwise manner with synthesis and insertion of the [4Fe–4S] subcluster occurring first, followed by synthesis of the 2Fe subcluster by specialized maturation machinery and insertion of the subcluster via a cationically charged channel that collapses following incorporation.

Date: 2010
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DOI: 10.1038/nature08993

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