Issue 7, 2017

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

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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Article information

Article type
Communication
Submitted
13 ม.ค. 2560
Accepted
11 เม.ย. 2560
First published
11 เม.ย. 2560
This article is Open Access
Creative Commons BY license

Energy Environ. Sci., 2017,10, 1563-1567

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, 10, 1563 DOI: 10.1039/C7EE00135E

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