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Inside Back Cover: Identification of the HcgB Enzyme in [Fe]‐Hydrogenase‐Cofactor Biosynthesis (Angew. Chem. Int. Ed. 48/2013)
Author(s) -
Fujishiro Takashi,
Tamura Haruka,
Schick Michael,
Kahnt Jörg,
Xie Xiulan,
Ermler Ulrich,
Shima Seigo
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201308951
Subject(s) - hydrogenase , cofactor , biosynthesis , guanosine , chemistry , enzyme , derivative (finance) , stereochemistry , biochemistry , financial economics , economics
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.