Title : Mechanistic studies on the intramolecular one-electron transfer between the two flavins in the human neuronal nitric-oxide synthase and inducible nitric-oxide synthase flavin domains.

Pub. Date : 2003 Aug 15

PMID : 12777376






4 Functional Relationships(s)
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Protein Name
Organism
1 Reduction of the air-stable semiquinone (FAD-FMNH*) of both domains with NADPH showed that the extent of conversion of FADH2/FMNH* to FADH*/FMNH2 in the iNOS flavin domain was greater than that of the nNOS flavin domain. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
2 Reduction of the air-stable semiquinone (FAD-FMNH*) of both domains with NADPH showed that the extent of conversion of FADH2/FMNH* to FADH*/FMNH2 in the iNOS flavin domain was greater than that of the nNOS flavin domain. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
3 The rate of intramolecular electron transfer between the two flavins in the iNOS flavin domain was faster than that of the nNOS flavin domain. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens
4 The rate of intramolecular electron transfer between the two flavins in the iNOS flavin domain was faster than that of the nNOS flavin domain. 4,6-dinitro-o-cresol nitric oxide synthase 1 Homo sapiens