The status of high-valent metal oxo complexes in the P450 cytochromes

被引：110
作者：
Makris, Thomas M.
von Koenig, Konstanze
Schlichting, Ilme
Sligar, Stephen G.
机构：
[1] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
[2] Univ Illinois, Dept Chem, Urbana, IL 61801 USA
[3] Univ Illinois, Sch Med, Urbana, IL 61801 USA
[4] Max Planck Inst Med Res, Abt Biomol Mech, D-69120 Heidelberg, Germany
来源：
JOURNAL OF INORGANIC BIOCHEMISTRY | 2006年 / 100卷 / 04期
关键词：
P450; compound I; ferryl; metal-oxo; X-ray;
D O I：
10.1016/j.jinorgbio.2006.01.025
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The oxidative prowess of the P450 cytochromes in physiological reactions is attributed to the production of a high-valent iron-oxo complex. or Compound I intermediate, in the reaction cycle. Despite many years of study, however, the full electronic description of this fleeting intermediate still remains an active area of study. In this manuscript, the current status of the isolation and characterization of the P450 oxo-Fe(IV) is examined and compared to analogous states in related heme enzymes. In addition, the utilization of cofactor exchange to stabilize high-valent oxo-states in the P450 is addressed. Structural and spectroscopic studies on manganese reconstituted P450, and its corresponding oxo-complex, are presented. (c) 2006 Elsevier Inc. All rights reserved.
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收藏
页码：507 / 518
页数：12
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