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Results 1 - 10 of 11 > >>
EC Number
Cofactor
Commentary
Reference
adrenodoxin
-
adrenodoxin
dependent on
cytochrome P450
-
cytochrome P450meg
it is possible to resolve the hydroxylase system into three proteins: a strictly NADPH-dependent FMN-containing flavoprotein (megaredoxin reductase), an iron-sulfur protein (megaredoxin), and cytochrome P-450 (P-450meg). The activity of the 15beta-hydroxylase system is fully reconstituted upon combination of these three proteins and addition of NADPH. Megaredoxin has an apparent sulfur to iron ratio of 0.98 and shows g-signals at 1.90, 1.93, and 2.06 when analyzed by electron paramagnetic resonance spectroscopy
Ferredoxin
-
heme
deoxycorticosterone binds in the heme pocket near the iron ligand
heme
presence of dehydroabietic acid does not induce a high-spin shift of the enzyme
heme
steroids beta-estradiol, estrone, pregnenolone and 17alpha-hydroxypregnenolone, do not shift the heme iron into the high-spin form; steroids beta-estradiol, estrone, pregnenolone and 17alpha-hydroxypregnenolone, do not shift the heme iron into the high-spin form
heme
the heme content of cytochrome P-450meg is 0.94 nmol of heme per nmol of cytochrome P-450
Results 1 - 10 of 11 > >>