Cytochrome P450 17A1 (CYP17A1) catalyzes the synthesis of androgens from the steroid precursors pregnenolone and progesterone in a two-step reaction process: allylic hydroxylation and carbo-carbon bond scission. Cytochrome b (Cyt-b ) is a stimulator of the second lyase reaction, but the chemical mechanism is unclear. We have shown previously that this stimulatory effect requires redox active Cyt-b . To investigate the origin of the lyase reaction enhancement by electron transfer from Cyt-b , we measured the reduction rates of oxy-ferrous substrate-bound CYP17A1 by Cyt-b and by cytochrome P450 reductase (CPR) coincorporated in Nanodiscs using stopped flow spectroscopy. We observed that Cyt-b reduces oxy-ferrous CYP17A1 10-fold faster than CPR, with the rate similar to that observed in a ternary complex of all three proteins.
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| http://dx.doi.org/10.1002/1873-3468.13153 | DOI Listing |
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