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

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.

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 Creators:
Watanabe, Tomohiro1, Author              
Wagner, Tristan1, Author              
Huang, Gangfeng1, Author              
Kahnt, Jörg2, Author              
Ataka, Kenichi3, Author
Ermler, Ulrich4, Author
Shima, Seigo1, Author              
Affiliations:
1Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              
2Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266266              
3Department of Physics, Freie Universität Berlin, 14195 Berlin, Germany, ou_persistent22              
4Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              

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Free keywords: Metalloenzymes; Protein structure; FeGP cofactor; Tetrahydrofolate; Tetrahydromethanopterin
 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

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Language(s): eng - English
 Dates: 2019-01-252019-03-11
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201813465
 Degree: -

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Title: Angewandte Chemie International Edition in English
  Abbreviation : Angew. Chem. Int. Ed. Engl.
Source Genre: Journal
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Publ. Info: Weinheim : Wiley-VCH
Pages: - Volume / Issue: 58 (11) Sequence Number: - Start / End Page: 3506 - 3510 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/0570-0833