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Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H2 supports its catalytic relevance.


ABSTRACT: Small molecules in solution may interfere with mechanistic investigations, as they can affect the stability of catalytic states and produce off-cycle states that can be mistaken for catalytically relevant species. Here we show that the hydride state (Hhyd), a proposed central intermediate in the catalytic cycle of [FeFe]-hydrogenase, can be formed in wild-type [FeFe]-hydrogenases treated with H2 in absence of other, non-biological, reductants. Moreover, we reveal a new state with unclear role in catalysis induced by common low pH buffers.

SUBMITTER: Senger M 

PROVIDER: S-EPMC9219605 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature

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Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H<sub>2</sub> supports its catalytic relevance.

Senger Moritz M   Kernmayr Tobias T   Lorenzi Marco M   Redman Holly J HJ   Berggren Gustav G  

Chemical communications (Cambridge, England) 20220623 51


Small molecules in solution may interfere with mechanistic investigations, as they can affect the stability of catalytic states and produce off-cycle states that can be mistaken for catalytically relevant species. Here we show that the hydride state (H<sub>hyd</sub>), a proposed central intermediate in the catalytic cycle of [FeFe]-hydrogenase, can be formed in wild-type [FeFe]-hydrogenases treated with H<sub>2</sub> in absence of other, non-biological, reductants. Moreover, we reveal a new stat  ...[more]

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