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In vivo activation of an [FeFe] hydrogenase using synthetic cofactors

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Abstract

[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.

Graphical abstract: In vivo activation of an [FeFe] hydrogenase using synthetic cofactors

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Publication details

The article was received on 13 Jan 2017, accepted on 11 Apr 2017 and first published on 11 Apr 2017


Article type: Communication
DOI: 10.1039/C7EE00135E
Citation: Energy Environ. Sci., 2017, Advance Article
  • Open access: Creative Commons BY license
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    In vivo activation of an [FeFe] hydrogenase using synthetic cofactors

    N. Khanna, C. Esmieu, L. S. Mészáros, P. Lindblad and G. Berggren, Energy Environ. Sci., 2017, Advance Article , DOI: 10.1039/C7EE00135E

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