Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802, USA.
J Biol Chem. 2013 Jun 14;288(24):17074-81. doi: 10.1074/jbc.R113.473108. Epub 2013 Apr 30.
Recently, we reported the spectroscopic and kinetic characterizations of cytochrome P450 compound I in CYP119A1, effectively closing the catalytic cycle of cytochrome P450-mediated hydroxylations. In this minireview, we focus on the developments that made this breakthrough possible. We examine the importance of enzyme purification in the quest for reactive intermediates and report the preparation of compound I in a second P450 (P450ST). In an effort to bring clarity to the field, we also examine the validity of controversial reports claiming the production of P450 compound I through the use of peroxynitrite and laser flash photolysis.
最近，我们报道了 CYP119A1 中细胞色素 P450 复合物 I 的光谱和动力学特征，有效地封闭了细胞色素 P450 介导的羟化作用的催化循环。在这篇综述中，我们重点介绍了促成这一突破的发展。我们研究了酶纯化在寻找反应中间体中的重要性，并报告了在第二种 P450（P450ST）中制备复合物 I 的情况。为了使该领域更加清晰，我们还研究了通过使用过氧亚硝酸盐和激光闪光光解产生 P450 复合物 I 的有争议报告的有效性。
