1.14.15.36	cytochrome P450	the oxidized absolute spectrum of the purified CYP51, in the absence of substrate, shows a Soret band at 417 nm and alpha-, beta-, and delta-bands at 569, 535, and 369 nm	
1.14.15.36	cytochrome P450	the oxidized absolute spectrum of the purified enzyme, in the absence of substrate, shows a Soret band at 417 nm and alpha-,beta-, and delta bands at 569, 535, and 369 nm	
1.14.15.36	Ferredoxin	-	
1.14.15.36	heme	heme-iron reduction is the rate limiting step in catalysis. Protonation of the cysteinate ligand to the ferrous CYP51 underlies the collapse of the Fe(II)-CO adduct of the enzyme from its P450 to its P420 form. The protonation is reversible and the rate of P420 formation is substantially retarded in the estriol-bound form of CYP51