1.14.15.8	adrenodoxin	-	693956	
1.14.15.8	adrenodoxin	dependent on	725584	
1.14.15.8	cytochrome P450	-	724061, 725584	
1.14.15.8	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	698682	
1.14.15.8	Ferredoxin	-	724061	
1.14.15.8	heme	-	696142, 725584	
1.14.15.8	heme	deoxycorticosterone binds in the heme pocket near the iron ligand	695980	
1.14.15.8	heme	presence of dehydroabietic acid does not induce a high-spin shift of the enzyme	744706	
1.14.15.8	heme	steroids beta-estradiol, estrone, pregnenolone and 17alpha-hydroxypregnenolone, do not shift the heme iron into the high-spin form	744148	
1.14.15.8	heme	the heme content of cytochrome P-450meg is 0.94 nmol of heme per nmol of cytochrome P-450	698682	
1.14.15.8	NADPH	-	693956, 698684