We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
The Bacterial [Fe]‐Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates.
- Authors
Watanabe, Tomohiro; Wagner, Tristan; Huang, Gangfeng; Kahnt, Jörg; Ataka, Kenichi; Ermler, Ulrich; Shima, Seigo
- 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, termed HmdII, and the HcgA–G proteins. The latter are required for the 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 hydrogenation of derivatives of tetrahydrofolate, the bacterial C1‐carrier, albeit with low enzymatic activities. The crystal structures show how Hmd recognizes tetrahydrofolate derivatives. These findings have an impact on future biotechnology by identifying a bacterial Hmd paralog.
- Subjects
HYDROGENASE; FOLIC acid; CHEMICAL derivatives; HYDROGENATION; PTERIDINES; ARCHAEBACTERIA
- Publication
Angewandte Chemie, 2019, Vol 131, Issue 11, p3544
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201813465