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• W1510335765 startingPage "114" @default.
• W1510335765 abstract "The biosynthesis of nitric oxide (NO) is catalyzed by nitric-oxide synthases (NOS). These enzymes are homodimers, in which each monomer consists of an oxygenase domain and a reductase domain that is homologous to cytochrome P-450 reductase. NOS catalyzes the transformation of L-arginine to L-citrulline and NO in two discrete steps, with NC-hydroxy-L-arginine (NHA) as intermediate. Both reactions take place at a P-450-type heme in the oxygenase domain and consume equivalent of O2. Both reactions also require electrons that are supplied by nicotinamide-adenine dinucleotide phosphate (NADPH) via two ravin moieties in the reductase domain. Reaction mechanisms proposed for the first step, the conversion of arginine to NHA, are based on the reaction cycle that is thought to describe P-450 catalysis. According to this model, ferric heme is reduced, binds O2, and accepts a second electron. This provides the energy to achieve O–O bond scission, expulsion of H20, and formation of oxyferryl heme. This compound hydroxylates arginine bound to the distal heme pocket, resulting in formation of NHA and regeneration of ferric heme. Because of the different electronic requirements of the second step, it has generally been assumed that hydroxylation of L-arginine and conversion of NHA to L-citrulline and NO must follow entirely different pathways." @default.
• W1510335765 created "2016-06-24" @default.
• W1510335765 creator A5022599009 @default.
• W1510335765 creator A5023053290 @default.
• W1510335765 creator A5040571384 @default.
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• W1510335765 date "2002-01-01" @default.
• W1510335765 modified "2023-10-16" @default.
• W1510335765 title "Redox Role for Tetrahydrobiopterin in Nitric Oxide Synthase Catalysis: Low-Temperature Optical Absorption Spectral Detection" @default.
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• W1510335765 doi "https://doi.org/10.1016/s0076-6879(02)53041-x" @default.
• W1510335765 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12078487" @default.
• W1510335765 hasPublicationYear "2002" @default.
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