Cytochrome P450cam (a camphor hydroxylase) isolated from soil bacterium Pseudomonas putida shows potent importance in environmental applications such as the degradation of chlorinated organic pollutants and insect control agents. Introducing such chemicals can be hazardous to the environment due to their lack of biodegradation. In this thesis, I have studied the role of several P450cam mutants in the oxidation of 3-chloroindole to isatin and the role of wild type P450cam in the dealkylation of 1,4-dibutoxybenzene, a potent feeding-deterrent against stored product pests. Mutant (E156G/V247F/V253G/F256S) was the most active in the conversion of 3-chloroindole by P450cam. We propose two mechanisms for the dechlorination of 3-chloroindole by P450cam. To investigate structure-activity patterns of 1,4-dialkoxybenzenes against beetles, the octanol-water partition coefficients of selected dialkoxybenzenes were investigated. Furthermore, P. putida strain ATCC17453 was able to metabolize 1,4-dibutoxybenzene. Results revealed that cytochrome P450cam catalyzed the first and second dealkylation steps in the biodegradation mechanism.
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Thesis advisor: Plettner, Erika
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