The equilibrium dissociation constants KD, the complex association / dissociation rate constants (kon / koff) and the lifetimes of redox partners' complexes were measured for three cytochrome P450-containing monooxygenase systems (P450cam, P450 2B4 and P450scc). To estimate the productivity of complexes formed within the systems studied, the Q parameter - i.e. the ratio of protein-protein complex lifetime (τLT) to the time required for a single hydroxylation cycle (τcat) - was determined. It was shown that Q was changed (albeit insignificantly) upon transition from the oxidation to hydroxylation conditions in all the three P450 - monooxygenase systems studied. It was shown that the binary complexes formed within the P450cam and the P450scc systems requiring an intermediate electron-transfer protein between the reductase and cytochrome P450 were non-productive while the binary complexes formed within the P450 2B4 system, not requiring such an intermediate electron-transfer protein, proved to be productive. Formation of ternary complexes within the three systems was demonstrated under hydroxylation conditions. Analysis of Q values led to the conclusion that the ternary complexes formed within the P450cam and the P450scc systems were virtually 100% productive. Within the P450 2B4 system, more than half (about 60%) ternary complexes were also found to be productive.
Ivanov Yu.D. et al. Productive and non-productive complexes in cytochrome P450-containing system // Biomeditsinskaya khimiya. - 2009. - V. 55. -N 3. - P. 310-330.
Ivanov Yu.D. et al., "Productive and non-productive complexes in cytochrome P450-containing system." Biomeditsinskaya khimiya 55.3 (2009): 310-330.
Ivanov, Yu. D., Ivanov, A. V., Kaysheva, A. L., Zgoda, V. G., Usanov, S. A., Hui-Bon-Hoa, G., Archakov, A. I. (2009). Productive and non-productive complexes in cytochrome P450-containing system. Biomeditsinskaya khimiya, 55(3), 310-330.
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