The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives 
as Substrates

Watanabe, Tomohiro; Wagner, Tristan; Huang, Gangfeng; Kahnt, Jörg; Ataka, Kenichi; Ermler, Ulrich; Shima, Seigo

doi:10.1002/anie.201813465

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The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates

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

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Citation

Watanabe, T., Wagner, T., Huang, G., Kahnt, J., Ataka, K., Ermler, U., et al. (2019). The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates. Angewandte Chemie International Edition in English, 58(11), 3506-3510. doi:10.1002/anie.201813465.

Cite as: https://hdl.handle.net/21.11116/0000-0003-8A16-9

Abstract

[Fe]‐hydrogenase (Hmd) catalyzes the reversible hydrogenation of methenyl‐tetrahydromethanopterin (methenyl‐H₄MPT⁺) with H₂. H₄MPT is a C1‐carrier of methanogenic archaea. One bacterial genus, Desulfurobacterium, contains putative genes for the Hmd paralog (HmdII) and the HcgA‐G proteins. The latter are involved in biosynthesis of the prosthetic group of Hmd, the iron‐guanylylpyridinol (FeGP) cofactor. This finding is intriguing because Hmd and HmdII strictly use H₄MPT derivatives that are absent in most bacteria. We identified the presence of the FeGP cofactor in D. thermolithotrophum. The bacterial HmdII reconstituted with the FeGP cofactor catalyzed the enzyme reactions using the tetrahydrofolate derivatives, which are the bacterial C1 carrier, albeit with low enzymatic activities. Crystal structure provided the basis for how the enzyme was adapted to the bacterial C1‐carrier. This finding has impact on future biotechnology by developing the Hmd variants functioning in Bacteria