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Angew Chem Int Ed Engl. 2015 Oct 12;54(42):12329-33. doi: 10.1002/anie.201502776. Epub 2015 Jun 12.

A redox hydrogel protects the O2 -sensitive [FeFe]-hydrogenase from Chlamydomonas reinhardtii from oxidative damage.

Author information

1
Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany).
2
Analytical Chemistry-Center for Electrochemical Sciences (CES), Ruhr-Universität Bochum, Universitätsstrasse 150, 44780 Bochum (Germany).
3
Lehrstuhl Biochemie der Pflanzen, AG Photobiotechnologie, Ruhr Universität Bochum, Universitätsstrasse 150, 44801 Bochum (Germany).
4
Max-Planck-Institut für Chemische Energiekonversion, Stiftstrasse 34-36, 45470 Mülheim an der Ruhr (Germany). olaf.ruediger@cec.mpg.de.
5
Center for Electrochemical Sciences-Molecular Nanostructures, Ruhr-Universität Bochum, Universitätsstrasse 150, 44780 Bochum (Germany). nicolas.plumere@rub.de.

Abstract

The integration of sensitive catalysts in redox matrices opens up the possibility for their protection from deactivating molecules such as O2 . [FeFe]-hydrogenases are enzymes catalyzing H2 oxidation/production which are irreversibly deactivated by O2 . Therefore, their use under aerobic conditions has never been achieved. Integration of such hydrogenases in viologen-modified hydrogel films allows the enzyme to maintain catalytic current for H2 oxidation in the presence of O2 , demonstrating a protection mechanism independent of reactivation processes. Within the hydrogel, electrons from the hydrogenase-catalyzed H2 oxidation are shuttled to the hydrogel-solution interface for O2 reduction. Hence, the harmful O2 molecules do not reach the hydrogenase. We illustrate the potential applications of this protection concept with a biofuel cell under H2 /O2 mixed feed.

KEYWORDS:

O2 protection; biocatalysis; biofuel cells; hydrogenases; viologen hydrogel

PMID:
26073322
DOI:
10.1002/anie.201502776
[Indexed for MEDLINE]

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