Ontology highlight
ABSTRACT:
SUBMITTER: Yukl ET
PROVIDER: S-EPMC2734454 | biostudies-literature | 2009 Jun
REPOSITORIES: biostudies-literature
Yukl Erik T ET de Vries Simon S Moënne-Loccoz Pierre P
Journal of the American Chemical Society 20090601 21
The dioxygenation of nitric oxide by oxyheme in globin proteins is a major route for NO detoxification in aerobic biological systems. In myoglobin, this reaction is thought to proceed through an iron(III)-bound peroxynitrite before homolytic cleavage of the O-O bond to form an iron(IV)-oxo and NO(2) radical followed by recombination and nitrate production. Single turnover experiments at alkaline pH have revealed the presence of a millisecond high-spin heme intermediate. It is widely presumed tha ...[more]