Cytochrome Bacillus megaterium

Berg A, JA Gustafsson, M Ingelman-Sundberg, K Carlstrdm (1976) Characterization of a cytochrome P-450-dependent steroid hydroxylase present in Bacillus megaterium. J Biol Chem 251 2831-2838. 

Narhi LO, AJ Fulco (1986) Characterization of a catalytically self-sufficient 119,000-Dalton cytochrome P-450 monooxygenase induced by barbiturates in Bacillus megaterium. J Biol Chem 261 7160-7169. 

P450 BM-3 cytochrome P450 BM-3 from Bacillus megaterium... 

It has been well recognized that the mixed-function oxidase system of Bacillus megaterium is involved in steroid hydroxylation (, as already described above. This enzyme system is composed of a NADPH-specific FMN flavoprotein (megaredoxin reductase), an iron-sulfur protein (megaredoxin) and cytochrome P cn. The megaredoxin protein plays an important role as an intermediate component of electron transfer from reduced flavoprotein to cytochrome P en. 

Narhi, L. O., and Fulco, A. J. (1987). Identification and characterization of two functional domains in cytochrome P-450BM-3, a catalytically self-sufficient monooxygenase induced by barbiturates in Bacillus megaterium. ]. Biol. Chem. 262, 6683-6690. 

Khan, K.K., Mazumdar, S., Modi, S., Sutcliffe, M., Roberts, G.C.K. and Mitra, S. (1997). Steady-state and picosecond-time-resolved fluorescence studies on the recombinant heme domain of Bacillus megaterium cytochrome P-450. European Journal of Biochemistry, 244, 361-370. 

Some Properties of a Self-Sufficient Cytochrome P-450 Monooxygenase System from Bacillus megaterium Strain ALA2... 

Matson, R. S., and Fulco, A. J. 1981. Hydroxystearates as Inhibitors of Palmitate Hydroxylation Catalyzed by the Cytochrome-P-450 Mono-Oxygenase from Bacillus megaterium. Biochem. Biophys. Res. Comm., 103, 531-535. 

Wen, L. P., Ruettinger, R. T., and Fulco, A. J. 1989. Requirement for a 1-Kilobase 5 -Flanking Sequence for Barbiturate-Inducible Expression of the Cytochrome P-450bm-3 Gene in Bacillus megaterium. J. Biol. Chem., 264,10996-11003. 

These screens have been used to direct the evolution of cytochrome P450 BM-3, a soluble enzyme from Bacillus megaterium that contains its reductase and hydroxylase domains on a single polypeptide chain. P450 BM-3 primarily catalyzes the hydroxylation of fatty acids ( 12 to 18 carbons long) at the a>-1, a>-2, and m-3 positions, but also... 

Epoxidation of various olefins by cytochrome P-450 enzymes has been studied using rat liver microsomes [29,30] as well as using enzymes from microbial origin. For example, Ruettinger and Fulco [31] reported the epoxidation of fatty acids such as palmitoleic acid by a cytochrome P-450 from Bacillus megaterium. Their results indicate that both the epoxidation and the hydroxylation processes are catalyzed by the same NADPH-dependent monooxygenase. More recently, other researchers demonstrated that the cytochrome P-450cam from Pseudomonas putida, which is known to hydroxylate camphor at a non-activated carbon atom, is also responsible for stereoselective epoxidation of cis- -methylstyrene [32]. The (lS,2R)-epoxide enantiomer obtained showed an enantiomeric purity (ee) of 78%. This result fits the predictions based on a theoretical approach (Fig. 2). 

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