Title : Calmodulin activates intramolecular electron transfer between the two flavins of neuronal nitric oxide synthase flavin domain.

Pub. Date : 1999 Dec 27

PMID : 10594372






3 Functional Relationships(s)
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1 The neuronal NO synthase (nNOS) flavin domain, which has similar redox properties to those of NADPH-cytochrome P450 reductase (P450R), contains binding sites for calmodulin, FAD, FMN, and NADPH. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
2 In this study, we used the recombinant nNOS flavin domains, which include or delete the calmodulin (CaM)-binding site. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
3 The air-stable semiquinone of the nNOS flavin domains showed similar redox properties to the corresponding FAD-FMNH(&z.ccirf;) of P450R. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens