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Genome of Streptomyces peucetius ATCC 27952 contains 23 cytochrome p450 genes. The ability of the cytochrome P450 heme monooxygenases to catalyze difficult oxidation reactions, often with high specificity and selectivity, makes them attractive for numerous biotechnological applications. However they are generally limited by low turnover rates and low stability, and their minimum requirements for catalysis include a cofactor as source of electrons (NAD(P)H), partner proteins for electron transfer, and dioxygen. Cytochrome P450 used in this study to investigate the hydroxylating property expressing in Escherichia coli belongs to the CYP105P2 family from S. peucetius. Owing to the inactivity of the isolated p450 enzymes,coexpression of three-component electron transfer chain in Escherichia coli was done from two plasmids with different selection markers and compatible origins of replication. The enzyme was supported in its activity with putidaredoxin reductase (CamA) and putidaredoxin (CamB) from Pseudomonas putida, supplying this enzyme with the reducing equivalents necessary in class I type electron transfer system. Hydroxylation of flavone ring was achieved as indicated by HPLC/GC-MS analysis.