Bacterial CYP154C8 catalyzes carbon-carbon bond cleavage in steroids
Bikash Dangi1, Tae-Jin Oh1,2,3
1Department of Life Science and Biochemical Engineering, SunMoon University, Asan-si, Korea.
Abstract:
Here, we report the first bacterial cytochrome P450, CYP154C8, that catalyzes the C-C bond cleavage reaction of steroids. A major change in product distribution is observed with CYP154C8, when the reactions are supported by NADPH and spinach redox partners ferredoxin and ferredoxin reductase, compared with previously reported reactions supported by NADH and redox partners containing putidaredoxin and putidaredoxin reductase. The NMR-based structural elucidation of reaction products reveals 21-hydroxyprednisone as the major product for prednisone, while the other product is identified as 1-dehydroadrenosterone obtained due to C-C bond cleavage. A similar pattern of product formation is observed with cortisone, hydrocortisone, and prednisone. The reaction catalyzed by CYP154C8 in the presence of oxygen surrogates also prominently shows the formation of C-C bond cleavage products.
Related Concept Videos
Carbon Skeletons
The Carbon Cycle
Carbonation Shrinkage
The concrete's permeability is slightly reduced as calcium carbonate produced during the reaction fills its pores. Furthermore, its strength is slightly enhanced as the water released during the reaction...
Carbon-dioxide Fixation
C–C Bond Cleavage: Retro-Aldol Reaction
In the first step, as depicted in Figure 1, the base deprotonates the β-hydroxy ketone at the hydroxyl group to form an alkoxide ion.
Carbon-13 (¹³C) NMR: Overview


