Electron supply and catalytic oxidation of nitrogen by cytochrome P450 and nitric oxide synthase.
Cytochrome P450 and nitric oxide synthase (NOS) oxidize nitrogen atoms, although the substrates and transformations are highly restricted for NOS. The first reaction catalyzed by NOS is mediated by a P450-like ferryl species, although it is generated by a distinct process in which a tetrahydrobiopterin molecule in NOS serves as a transient electron donor. The second NOS reaction appears to be mediated by an iron dioxygen precursor of the ferryl species. The transient tetrahydrobiopterin radical formed in these reactions is quenched by electron transfer from the NOS flavin domain. Electron transfer from the flavins is controlled by the binding of calmodulin, the presence of peptide inserts in the flavin domain, the substrate structure, and phosphorylation of the enzyme.
Nishida
Clinton R
CR
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446, USA.
Knudsen
Giselle
G
Straub
Wesley
W
Ortiz de Montellano
Paul R
PR
D001120:Arginine / Q000378:metabolism; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D004579:Electron Transport; D006419:Heme Oxygenase (Decyclizing) / Q000737:chemistry / Q000378:metabolism; D007501:Iron / Q000378:metabolism; D008958:Models, Molecular; D015394:Molecular Structure; D019001:Nitric Oxide Synthase / Q000737:chemistry / Q000378:metabolism*; D009584:Nitrogen / Q000378:metabolism*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism; D017434:Protein Structure, Tertiary
D003577:Cytochrome P-450 Enzyme System; D001120:Arginine; D007501:Iron; D019001:Nitric Oxide Synthase; D006419:Heme Oxygenase (Decyclizing); D009584:Nitrogen; D010100:Oxygen