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Reactivation of sulfide-protected [FeFe] hydrogenase in a redox-active hydrogel

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Rüdiger,  Olaf
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Birrell,  James A.
Research Department DeBeer, Max Planck Institute for Chemical Energy Conversion, Max Planck Society;

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Citation

Oughli, A. A., Hardt, S., Rüdiger, O., Birrell, J. A., & Plumer, N. (2020). Reactivation of sulfide-protected [FeFe] hydrogenase in a redox-active hydrogel. Chemical Communications, 56(69), 9958-9961. doi:10.1039/d0cc03155k.


Cite as: http://hdl.handle.net/21.11116/0000-0007-D336-E
Abstract
[FeFe] hydrogenases are highly active hydrogen conversion catalysts but are notoriously sensitive to oxidative damage. Redox hydrogels have been used for protecting hydrogenases from both high potential inactivation and oxygen inactivation under turnover conditions. However, [FeFe] hydrogenase containing redox hydrogels must be fabricated under strict anoxic conditions. Sulfide coordination at the active center of the [FeFe] hydrogenase from Desulfovibrio desulfuricans protects this enzyme from oxygen in an inactive state, which can be reactivated upon reduction. Here, we show that this oxygen-stable inactive form of the hydrogenase can be reactivated in a redox hydrogel enabling practical use of this highly O-2 sensitive enzyme without the need for anoxic conditions.