STUDIES ON THE ACTIVE SITES OF CYTOCHROMES P-450

细胞色素P-450a是一种P-450同工酶，表现出高度的 7α-羟化类固醇的区域特异性。这个 导致这一现象的空间和电子结合性质 特异性将通过评估几种新陈代谢来探讨 类固醇类似物或片断。本研究中使用的模型包括 脂族和不饱和环系类固醇碎片，以及 潜在的结合血红素的光学活性类固醇类似物。这个 区域选择性、手性和前手性选择性及动力学 这些底物的新陈代谢将被用于评估 P-450a活性中心的几何性质。

Cytochrome P-450a is a P-450 isozyme showing a high degree of regiospecificity of the 7 alpha-hydroxylation of steroids. The steric and electronic binding properties responsible for this specificity will be probed by evaluating the metabolism of several steroid analogs or fragments. Models used in this study include aliphatic and unsaturated ring systems steroid fragments, and a potential heme-binding optically active steroid analog. The regioselectivity, chiral and prochiral selectivity, and kinetics of the metabolism of these substrates will be used to evaluate the geometric properties of the P-450a active site.