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In vivo activation of an [FeFe] hydrogenase using synthetic cofactors
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
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2017 (English)In: Energy & Environmental Science, ISSN 1754-5692, E-ISSN 1754-5706, Vol. 10, no 7, 1563-1567 p.Article in journal (Refereed) Published
Abstract [en]

[FeFe] hydrogenases catalyze the reduction of protons, and oxidation of hydrogen gas, with remarkable efficiency. The reaction occurs at the H-cluster, which contains an organometallic [2Fe] subsite. The unique nature of the [2Fe] subsite makes it dependent on a specific set of maturation enzymes for its biosynthesis and incorporation into the apo-enzyme. Herein we report on how this can be circumvented, and the apo-enzyme activated in vivo by synthetic active site analogues taken up by the living cell.

Place, publisher, year, edition, pages
2017. Vol. 10, no 7, 1563-1567 p.
National Category
Chemical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-330015DOI: 10.1039/c7ee00135eISI: 000405279900003OAI: oai:DiVA.org:uu-330015DiVA: diva2:1148521
Funder
Swedish Research Council, 621-2014-5670Swedish Research Council Formas, 213-2014-880Swedish Energy Agency, 11674-5Knut and Alice Wallenberg Foundation, 2011.0067Wenner-Gren Foundations
Available from: 2017-10-11 Created: 2017-10-11 Last updated: 2017-10-11Bibliographically approved

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Khanna, NamitaEsmieu, CharlèneMeszaros, Livia S.Lindblad, PeterBerggren, Gustav

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