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          Institute: MPI für Biophysik     Collection: Abt. Molekulare Membranbiologie     Display Documents



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ID: 680427.0, MPI für Biophysik / Abt. Molekulare Membranbiologie
Identification of the HcgB Enzyme in [Fe]-Hydrogenase-Cofactor Biosynthesis
Authors:Fujishiro, Takashi; Tamura, Haruka; Schick, Michael; Kahnt, Jörg; Xie, Xiulan; Ermler, Ulrich; Shima, Seigo
Language:English
Date of Publication (YYYY-MM-DD):2013-11-25
Title of Journal:Angwandte Chemie International Edition
Journal Abbrev.:Ang. Chem. Int. Ed.
Volume:52
Issue / Number:48
Start Page:12555
End Page:12558
Review Status:Peer-review
Audience:Experts Only
Abstract / Description:One reaction step of the biosynthesis of [Fe]-hydrogenase-cofactor is elucidated by S. Shima et al. in their Communication on page 12555 ff. A structural genomics approach, in combination with model reactions and thorough product analysis by X-ray crystallography of the protein–product complexes, revealed that HcgB is the enzyme that catalyzes guanylylpyridinol formation from a 2,4-dihydroxypyridine derivative and guanosine triphosphate.
Free Keywords:biosynthesis; cofactors, hydrogenases; protein structures; transferases
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Molekulare Membranbiologie
MPI für terrestrische Mikrobiologie/Department-independent groups
External Affiliations:Department of Chemistry, Philipps-Universität Marburg, Hans-Meerwein Strasse, 35032 Marburg, Germany
PRESTO, Japan Science and Technology Agency (JST) Honcho, Kawaguchi, Saitama 332-0012, Japan
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