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The Cofactor of the Iron–Sulfur Cluster Free Hydrogenase Hmd: Structure of the Light‐Inactivation Product
Author(s) -
Shima Seigo,
Lyon Erica J.,
SordelKlippert Melanie,
Kauß Manuela,
Kahnt Jörg,
Thauer Rudolf K.,
Steinbach Klaus,
Xie Xiulan,
Verdier Laurent,
Griesinger Christian
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200353763
Subject(s) - cofactor , hydrogenase , chemistry , chromophore , iron–sulfur cluster , sulfur , cluster (spacecraft) , nuclear magnetic resonance spectroscopy , metalloprotein , mass spectrometry , stereochemistry , spectroscopy , photochemistry , crystallography , enzyme , biochemistry , organic chemistry , physics , computer science , programming language , chromatography , quantum mechanics
A combination of NMR spectroscopy and mass spectrometry has been crucial in determining the structure of the relatively stable light‐inactivated form of the cofactor of the hydrogenase Hmd (see scheme). These studies have shown that the chromophore bound to GMP through a phosphoester linkage is a pyridone derivative.