Recombinant Rat NADPH--cytochrome P450 reductase (Por)

1. The structure of four-electron-reduced, NADP(+)-bound wild type CYPOR shows the plane of the nicotinamide ring positioned perpendicular to the FAD isoalloxazine with its carboxamide group forming H-bonds with N1 of the flavin ring and the Thr535 hydroxyl group. PMID: 29308883
2. the N-terminus of CYP2J2 is very important to form a productive CYP-CPR complex to facilitate electron transfer. PMID: 25450017
3. Data suggest CYP17A1, with electron donor NADPH-P450 reductase, is inherently distributive enzyme but that some processivity is present; some 17alpha-hydroxy pregnenolone formed does not dissociate from CYP17A1 before conversion to dehydroepiandrosterone; CYB5A does not enhance reaction by decreasing k(off) of ligands of CYP17A1. (CYP17A1 = cytochrome P450, family 17, subfamily A, polypeptide 1; CYB5A = cytochrome b5) PMID: 28684414
4. The DeltaGly-143 protein had moderately decreased activity with cytochrome P450 and cytochrome c. It formed a flexible loop, which transiently interacts with the flavin N5, resulting in the generation of both an unstable neutral blue semiquinone and hydroquinone. PMID: 27189945
5. the structure and dynamics of the full-length NADPH-cytochrome P450 oxidoreductase PMID: 24853741
6. Study of the role of P450 hydrophobic residues in complex formation with CPR uncovers novel roles for surface-exposed residues Val267 and Leu270 of CYP2B4 in mediating CYP2B4-CPR interactions. PMID: 21462923
7. Conformational changes of NADPH-cytochrome P450 oxidoreductase are essential for catalysis and cofactor binding. PMID: 21345800
8. Studies indicate that CPR conformational changes involving a combination of a "swinging" and "rotating" model and enables CPR to serve as an effective electron transferring "nano-machine". PMID: 20624491
9. Lipid bilayer has a role in defining the redox potential of the cytochrome P450 reductase flavin domains. PMID: 19908820
10. Importance of the direct NADPH-dependent reduction of superoxide-sensitive probes by cytochrome P450-reductase even though this enzyme does not, on its own accord, produce reactive oxygen species. PMID: 15031143
11. origin of the NOS enzymes from modules consisting of a heme domain and POR or ferredoxin-NADP(+) reductase- and flavodoxin-like subdomains that constitute POR, followed by recruitment of smaller modulating elements into the flavin-binding domains PMID: 16249336
12. cytochrome P450 reductase competes with cytochrome b5 for a binding site on cytochrome P450 2B4 PMID: 17693640
13. We present for the first time evidences that the choroids plexus express transcripts for both UGT1A6 and NADPH-cytochrome P450 reductase PMID: 19023562
14. Purification of of a membrane-bound protein yielded CYPOR PMID: 19152507
15. Bone malformations associated with defective cytochrome P450 oxidoreductase activity are due to reduced cholesterol synthesis and, in turn, reduced Indian hedgehog expression in chondrocytes. PMID: 19264869

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KEGG: rno:29441

STRING: 10116.ENSRNOP00000001961

UniGene: Rn.11359