Sulfide Protects [FeFe] Hydrogenases From O2

Sulfide Protects [FeFe] Hydrogenases From O2

[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 Hox air....

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Veröffentlicht in:Journal of the American Chemical Society 2018-08, Vol.140 (30), p.9346-9350
Hauptverfasser: Rodríguez-Maciá, Patricia, Reijerse, Edward J, van Gastel, Maurice, DeBeer, Serena, Lubitz, Wolfgang, Rüdiger, Olaf, Birrell, James A
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container_end_page 9350
container_issue 30
container_start_page 9346
container_title Journal of the American Chemical Society
container_volume 140
creator Rodríguez-Maciá, Patricia
Reijerse, Edward J
van Gastel, Maurice
DeBeer, Serena
Lubitz, Wolfgang
Rüdiger, Olaf
Birrell, James A
description [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 Hox air. The formation of the Hox air 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 Hox air state in DdHydAB and the [FeFe] hydrogenase from Chlamydomonas reinhardtii, which is based on high potential inactivation in the presence of sulfide.
doi_str_mv 10.1021/jacs.8b04339
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