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The Bacterial [Fe]-Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates.
- Source :
-
Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2019 Mar 11; Vol. 58 (11), pp. 3506-3510. Date of Electronic Publication: 2019 Jan 25. - Publication Year :
- 2019
-
Abstract
- [Fe]-hydrogenase (Hmd) catalyzes the reversible hydrogenation of methenyl-tetrahydromethanopterin (methenyl-H <subscript>4</subscript> MPT <superscript>+</superscript> ) with H <subscript>2</subscript> . H <subscript>4</subscript> MPT 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 H <subscript>4</subscript> MPT 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.<br /> (© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.)
- Subjects :
- Biocatalysis
Crystallization
Guanine analogs & derivatives
Guanine biosynthesis
Hydrogenation
Oxidation-Reduction
Protein Binding
Protein Conformation
Pyridines
Bacteria enzymology
Bacterial Proteins metabolism
Hydrogenase metabolism
Iron-Sulfur Proteins metabolism
Tetrahydrofolates chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1521-3773
- Volume :
- 58
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Angewandte Chemie (International ed. in English)
- Publication Type :
- Academic Journal
- Accession number :
- 30600878
- Full Text :
- https://doi.org/10.1002/anie.201813465