酵母微粒体中表达的人细胞色素P-450 3A4底物结合和自旋转变的热力学研究。
Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes.
作者信息
Renaud J P, Davydov D R, Heirwegh K P, Mansuy D, Hui Bon Hoa G H
机构信息
CNRS URA 400, Universite Rene Descartes, Paris, France.
出版信息
Biochem J. 1996 Nov 1;319 ( Pt 3)(Pt 3):675-81. doi: 10.1042/bj3190675.
Abstract
An approach to the quantitative spectral analysis of substrate binding and inactivation of cytochrome P-450 in microsomes is described. The method is based on the application of the principal component analysis technique on the Soret-region spectra measured at different temperatures at various concentrations of substrate. This approach allowed us to study the thermodynamic parameters of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast (Saccharomyces cerevisiae) microsomes. These parameters are discussed in comparison with the values reported earlier by Ristau et al. [(1979) Acta Biol. Med. Ger. 38, 177-185] for rabbit liver cytochrome P-450 2B4 in solution with benzphetamine as a substrate. Our analysis shows the substrate-free states of 2B4 and 3A4 to be very similar. However, substrate binding seems to perturb haem-protein interactions in 3A4 in contrast with 2B4, where the effect of substrate binding on the thermodynamic parameters of spin transitions was insignificant. The implication of the results for the mechanism of substrate-induced spin shift is discussed.
摘要
本文描述了一种对微粒体中细胞色素P - 450底物结合和失活进行定量光谱分析的方法。该方法基于对在不同温度、不同底物浓度下测得的Soret区光谱应用主成分分析技术。这种方法使我们能够研究在酵母（酿酒酵母）微粒体中表达的人细胞色素P - 450 3A4的底物结合热力学参数和自旋转变。将这些参数与Ristau等人[（1979年）《德国生物医学学报》38卷，177 - 185页]早期报道的以苄非他明为底物的兔肝细胞色素P - 450 2B4溶液中的值进行了比较讨论。我们的分析表明2B4和3A4的无底物状态非常相似。然而，与2B4相反，底物结合似乎扰乱了3A4中的血红素 - 蛋白质相互作用，在2B4中底物结合对自旋转变热力学参数的影响不显著。讨论了这些结果对底物诱导自旋位移机制的意义。
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