title: Active intermediates in heme monooxygenase reactions as revealed by cryoreduction/annealing, EPR/ENDOR studies.
abstract: This review describes the use of cryoreduction/annealing EPR/ENDOR techniques for determining the active oxidizing species in reactions catalyzed by heme monooxygenases. The three candidate heme states are: ferric peroxo, ferric hydroperoxo and compound I intermediates. The enzymes discussed include cytochromes P450, nitric oxide synthase and heme oxygenase.
authors.affiliation: Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.
authors.forename: Roman
authors.initials: R
authors.lastname: Davydov
authors.forename: Brian M
authors.initials: BM
authors.lastname: Hoffman
mesh_terms: D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy / Q000379:methods*; D004789:Enzyme Activation; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D019001:Nitric Oxide Synthase / Q000737:chemistry / Q000378:metabolism*
chemical_list: D003577:Cytochrome P-450 Enzyme System; D019001:Nitric Oxide Synthase; D006419:Heme Oxygenase (Decyclizing)