Abstract
The cotton bollworm, Helicoverpa armigera, is a polyphagous pest that has a strong capacity to evolve resistance against various classes of insecticides. Cytochrome P450 enzymes have been suspected involved in pyrethroid metabolism and resistance in this pest. However, how many and which P450s are involved in pyrethroid metabolism is largely unknown. In this study, CYP6B6 and NADPH-cytochrome P450 reductase (HaCPR) from H. armigera were successfully co-expressed in Escherichia coli. Incubation of esfenvalerate with the recombinant CYP6B6-HaCPR monooxygenase complex revealed that CYP6B6 was able to transform esfenvalerate into 4′-hydroxy fenvalerate. Kcat and Km values for the formation of 4′-hydroxyfenvalerate by the E. coli-produced CYP6B6 were determined to be 1.65±0.11min−1 and 4.10±0.84μM respectively. Our results demonstrate that CYP6B6 has the ability to hydroxylate esfenvalerate, thus plays a role in fenvalerate detoxification.
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