Ontology highlight
ABSTRACT:
SUBMITTER: Wagener N
PROVIDER: S-EPMC2708692 | biostudies-literature | 2009 Jul
REPOSITORIES: biostudies-literature
Proceedings of the National Academy of Sciences of the United States of America 20090622 27
Nicotinate dehydrogenase (NDH) from Eubacterium barkeri is a molybdoenzyme catalyzing the hydroxylation of nicotinate to 6-hydroxynicotinate. Reactivity of NDH critically depends on the presence of labile (nonselenocysteine) selenium with an as-yet-unidentified form and function. We have determined the crystal structure of NDH and analyzed its active site by multiple wavelengths anomalous dispersion methods. We show that selenium is bound as a terminal Mo=Se ligand to molybdenum and that it occu ...[more]