Issue 7, 2017
From the journal:

Energy & Environmental Science

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

N. Khanna,‡a   C. Esmieu,‡b   L. S. Mészáros,‡b   P. Lindblad*a  and  G. Berggren ORCID logo *b  

* Corresponding authors

a Microbial Chemistry, Department of Chemistry – Ångström Laboratory, Uppsala University, Uppsala, Sweden
E-mail: peter.lindblad@kemi.uu.se

b Molecular Biomimetics, Department of Chemistry – Ångström Laboratory, Uppsala University, Uppsala, Sweden
E-mail: gustav.berggren@kemi.uu.se

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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DOI
https://doi.org/10.1039/C7EE00135E
Article type
Communication
Submitted
13 Jan 2017
Accepted
11 Apr 2017
First published
11 Apr 2017
This article is Open Access
Creative Commons BY license

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

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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, 10, 1563 DOI: 10.1039/C7EE00135E

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