Davydov R M, Khanina O Iu, Iagofarov S, Uvarov V Iu, Archakov A I
Biokhimiia. 1986 Jan;51(1):125-9.
Using the flash photolysis technique, it was found that the kinetics of recombination of carbon monoxide with ferrocytochrome P-450 LM-2 can be approximated by the sum of three exponents. Incorporation of cytochrome P-450 into liposomes prepared from microsomal lipids leads to the reduction of the number of steps to two as well as to essential changes in rate constants. Addition of type I substrates (Triton N-101, albumin) cause similar changes in the reaction kinetics. NADPH-cytochrome P-450 reductase has no effect on this process. The multistep kinetics of CO recombination with cytochrome P-450 LM-2 may be accounted for by the presence of some protein conformers. The experimental results suggest that the activity and structure of cytochrome P-450 conformers is affected by the lipid microenvironment, type I substrates and Triton N-101.
利用闪光光解技术发现，一氧化碳与亚铁细胞色素P - 450 LM - 2的重组动力学可用三个指数之和来近似。将细胞色素P - 450掺入由微粒体脂质制备的脂质体中会导致步骤数减少到两个，同时速率常数也发生了本质变化。添加I型底物（曲拉通N - 101、白蛋白）会使反应动力学发生类似变化。NADPH - 细胞色素P - 450还原酶对该过程没有影响。一氧化碳与细胞色素P - 450 LM - 2重组的多步动力学可能是由于存在一些蛋白质构象异构体。实验结果表明，细胞色素P - 450构象异构体的活性和结构受脂质微环境、I型底物和曲拉通N - 101的影响。
