| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1925484 | Archives of Biochemistry and Biophysics | 2012 | 18 Pages |
Abstract
⺠This review covers structure and mechanism of NADPH-cytochrome P450 oxidoreductase and the reductase domains of nitric oxide synthases. ⺠The enzymes catalyze electron transfer from NADPH to FAD to FMN to the heme center of cytochrome P450 or of the NOS oxygenase domains. ⺠The enzymes contain distinct FAD and FMN domains that are connected by a flexible hinge. ⺠Two flavin domains undergo large domain movements during catalysis.
Keywords
MSRP450BM3(6R)-5,6,7,8-TetrahydrobiopterinFerredoxin-NADP+ oxidoreductaseFlavinsNOSoxyH4BFNRcyt b5FLDP450Cyt CeNOSnNOSiNOSNOSneuronal NOSinducible NOSelectron transferCAMcytochrome b5cytochrome cCytochrome P450endoplasmic reticulumFlavodoxinMethionine synthasemethionine synthase reductasemenadionenitric oxide synthaseHemeCalmodulin
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Authors
Takashi Iyanagi, Chuanwu Xia, Jung-Ja P. Kim,