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Journal Article

Dioxygen Sensitivity of [Fe]‐Hydrogenase in the Presence of Reducing Substrates


Ermler,  Ulrich       
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Huang, G., Wagner, T., Ermler, U., Bill, E., Ataka, K., & Shima, S. (2018). Dioxygen Sensitivity of [Fe]‐Hydrogenase in the Presence of Reducing Substrates. Angewandte Chemie International Edition in English, 57(18), 4917-4920. doi:10.1002/anie.201712293.

Cite as: https://hdl.handle.net/21.11116/0000-0002-668A-0
Mono‐iron hydrogenase ([Fe]‐hydrogenase) reversibly catalyzes the transfer of a hydride ion from H2 to methenyltetrahydromethanopterin (methenyl‐H4MPT+) to form methylene‐H4MPT. Its iron guanylylpyridinol (FeGP) cofactor plays a key role in H2 activation. Evidence is presented for O2 sensitivity of [Fe]‐hydrogenase under turnover conditions in the presence of reducing substrates, methylene‐H4MPT or methenyl‐H4MPT+/H2. Only then, H2O2 is generated, which decomposes the FeGP cofactor; as demonstrated by spectroscopic analyses and the crystal structure of the deactivated enzyme. O2 reduction to H2O2 requires a reductant, which can be a catalytic intermediate transiently formed during the [Fe]‐hydrogenase reaction. The most probable candidate is an iron hydride species; its presence has already been predicted by theoretical studies of the catalytic reaction. The findings support predictions because the same type of reduction reaction is described for ruthenium hydride complexes that hydrogenate polar compounds