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Spontaneous activation of [FeFe]-hydrogenases by an inorganic [2Fe] active site mimic
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2013 (English)In: Nature Chemical Biology, ISSN 1552-4450, E-ISSN 1552-4469, Vol. 9, no 10, 607-609 p.Article in journal (Refereed) Published
Abstract [en]

Hydrogenases catalyze the formation of hydrogen. The cofactor ('H-cluster') of [FeFe]-hydrogenases consists of a [4Fe-4S] cluster bridged to a unique [2Fe] subcluster whose biosynthesis in vivo requires hydrogenase-specific maturases. Here we show that a chemical mimic of the [2Fe] subcluster can reconstitute apo-hydrogenase to full activity, independent of helper proteins. The assembled H-cluster is virtually indistinguishable from the native cofactor. This procedure will be a powerful tool for developing new artificial H-2-producing catalysts.

Place, publisher, year, edition, pages
2013. Vol. 9, no 10, 607-609 p.
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-95423DOI: 10.1038/NCHEMBIO.1311ISI: 000325041800006OAI: oai:DiVA.org:su-95423DiVA: diva2:660856
Funder
EU, FP7, Seventh Framework Programme, 306398
Note

AuthorCount:13;

Available from: 2013-10-31 Created: 2013-10-28 Last updated: 2017-12-06Bibliographically approved

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