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Sulfide Protects [FeFe] Hydrogenases From O2

MPG-Autoren
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van Gastel,  Maurice
Research Group van Gastel, Max-Planck-Institut für Kohlenforschung, Max Planck Society;

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Zitation

Rodríguez-Maciá, P., Reijerse, E. J., van Gastel, M., DeBeer, S., Lubitz, W., Rüdiger, O., et al. (2018). Sulfide Protects [FeFe] Hydrogenases From O2. Journal of the American Chemical Society, 140(30), 9346-9350. doi:10.1021/jacs.8b04339.


Zitierlink: http://hdl.handle.net/21.11116/0000-0002-0592-3
Zusammenfassung
[FeFe] hydrogenases catalyze proton reduction and hydrogen oxidation with high rates and efficiency under physiological conditions, but are highly oxygen sensitive. The [FeFe] hydrogenase from Desulfovibrio desulfuricans (DdHydAB) can be purified under air in an oxygen stable inactive state Hoxair. The formation of the Hoxair state in vitro allows the handling of hydrogenases in air, making their implementation in biotechnological applications more feasible. Here, we report a simple and robust protocol for the formation of the Hoxair state in DdHydAB and the [FeFe] hydrogenase from Chlamydomonas reinhardtii, which is based on high potential inactivation in the presence of sulfide.