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Issue 1, 2011
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Towards engineering O2-tolerance in [Ni–Fe] hydrogenases

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Abstract

Hydrogenases catalyze the conversion between 2H+ + 2e and H2. Most of these enzymes are inhibited by O2, which represents a major drawback for their use in biotechnological applications. Improving hydrogenase O2 tolerance is therefore a major contemporary challenge to allow the implementation of a sustainable hydrogen economy. A few bacteria, however, contain hydrogenases that activate H2 even in the presence of O2. Intriguingly, kinetic and spectroscopic studies lead to assuming that different mechanisms might be responsible for the resistance, depending on the enzyme type. The various hypotheses that emerged from these studies are still a matter of debate. In order to better understand the molecular bases of resistance to O2 inhibition, we explored different methods to improve the O2-tolerance of the O2-sensitive [Ni–Fe] hydrogenase from Desulfovibrio fructosovorans. A whole bunch of mutants has been studied and fully characterized, which revealed that actually, different mechanisms can lead to O2 tolerance. These mechanisms are described in this review and compared to the current hypothesis of O2 tolerance.

Graphical abstract: Towards engineering O2-tolerance in [Ni–Fe] hydrogenases

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Article information


Submitted
26 May 2010
Accepted
20 Aug 2010
First published
26 Oct 2010

Energy Environ. Sci., 2011,4, 33-41
Article type
Review Article

Towards engineering O2-tolerance in [Ni–Fe] hydrogenases

P. Liebgott, S. Dementin, C. Léger and M. Rousset, Energy Environ. Sci., 2011, 4, 33
DOI: 10.1039/C0EE00093K

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