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

[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 fo...

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Bibliographic Details
Published in:Energy & environmental science 2017-07, Vol.10 (7), p.1563-1567
Main Authors: Khanna, N., Esmieu, C., Mészáros, L. S., Lindblad, P., Berggren, G.
Format: Article
Language:English
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Summary:[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.
ISSN:1754-5692
1754-5706
1754-5706
DOI:10.1039/C7EE00135E