English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

[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.

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