In vivo activation of an [FeFe] hydrogenase using synthetic cofactorsElectronic supplementary information (ESI) available: Including genetic constructs, strains, Western blots and additional hydrogenase assays. See DOI: 10.1039/c7ee00135e

[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
Main Authors: Khanna, N, Esmieu, C, Mészáros, L. S, Lindblad, P, Berggren, G
Format: Article
Language:English
Online Access:Get full text
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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. The [FeFe]-hydrogenase can incorporate synthetic cofactors inside living cells, allowing for artificial enzyme activation under in vivo conditions.
ISSN:1754-5692
1754-5706
DOI:10.1039/c7ee00135e