Bernhardt R, Makower A, Jänig G R, Ruckpaul K
Biochim Biophys Acta. 1984 Mar 29;785(3):186-90. doi: 10.1016/0167-4838(84)90143-2.
Fluorescein isothiocyanate (FITC) has been selectively bound to the epsilon-amino group of lysine-382 in cytochrome P-450 LM2 (RH, reduced-flavoprotein: oxygen oxidoreductase (RH-hydroxylating), EC 1.14.14.1) at pH 8.15. Benzphetamine N-demethylase activity of the reconstituted FITC-modified cytochrome P-450 LM2 was inhibited by 25%. This inhibition has been shown to be due to an impaired electron transfer from the NADPH-cytochrome P-450 reductase (NADPH: ferricytochrome oxidoreductase, EC 1.6.2.4) to the haemoprotein. The data indicate that cytochrome P-450 interacts with the flavoprotein via electrostatic interactions.
在pH 8.15条件下，异硫氰酸荧光素（FITC）已选择性地结合到细胞色素P-450 LM2（RH，还原黄素蛋白：氧氧化还原酶（RH-羟化），EC 1.14.14.1）中赖氨酸-382的ε-氨基上。重组的FITC修饰细胞色素P-450 LM2的苄非他明N-脱甲基酶活性被抑制了25%。已证明这种抑制是由于从NADPH-细胞色素P-450还原酶（NADPH：铁细胞色素氧化还原酶，EC 1.6.2.4）到血红素蛋白的电子传递受损所致。数据表明细胞色素P-450通过静电相互作用与黄素蛋白相互作用。
