Abstract
P450 enzymes are known for catalyzing hydroxylation reactions of non-activated C-H bonds. For example, P450cam from Pseudomonas putida oxidizes (1R)-(+)-camphor to 5-exo-hydroxy camphor and further to 5-ketocamphor. This hydroxylation reaction proceeds via a catalytic cycle in which the reduction of dioxygen (O2) is coupled to the oxidation of the substrate. We have observed that under conditions of low oxygen, P. putida and isolated P450cam reduce camphor to borneol. We characterized the formation of borneol under conditions of low oxygen or when the catalytic cycle is shunted by artificial oxidants like m-chloro perbenzoic acid, cumene hydroperoxide, etc. We also tested the toxicity of camphor and borneol with P. putida and Escherichia coli. We have found that in P. putida borneol is less toxic than camphor, whereas in E. coli borneol is more toxic than camphor. We discuss a potental ecological advantage of the camphor reduction reaction for P. putida.
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Notes
Scifinder search (25th January, 2011) for whether the organisms E. coli and P. putida compete with each another in nature yielded no references.
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Acknowledgments
This work was supported by NSERC (Discovery grant No. 222923-05). We thank the Chem 381 class (Spring 2006) for help in isolating products from P. putida. B. Prasad performed experiments with the purified P450cam system, with camphor/borneol toxicity, the IC50 experiments and wrote the paper. A. Rojubally performed the standard syntheses and time course experiments with P. putida. E. Plettner designed and planned the project.
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Prasad, B., Rojubally, A. & Plettner, E. Identification of Camphor Oxidation and Reduction Products in Pseudomonas putida: New Activity of the Cytochrome P450cam System. J Chem Ecol 37, 657–667 (2011). https://doi.org/10.1007/s10886-011-9959-7
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DOI: https://doi.org/10.1007/s10886-011-9959-7