Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes

被引：79

作者：

Kuehnel, Karin

Derat, Etienne

Terner, James

Shaik, Sason ^{[1
]}

Schlichting, Ilme

机构：

[1] Hebrew Univ Jerusalem, Lise Meitner Minerva Ctr Computat Quantum Chem, Dept Organ Chem, IL-91904 Jerusalem, Israel

[2] Max Planck Inst Med Res, Dept Biomol Mech, D-69120 Heidelberg, Germany

[3] Virginia Commonwealth Univ, Dept Chem, Richmond, VA 23284 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2007年 / 104卷 / 01期

关键词：

crystal structure; protein structure/function; radiolysis; reaction mechanism; QM/MM calculations;

D O I：

10.1073/pnas.0606285103

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

We have determined the crystal structure of the chloroperoxidase (CPO) hydroperoxo reaction intermediate (CPO compound O) at 1.75-angstrom resolution. The intermediate was generated through controlled photoreduction of the CPO oxygen complex during x-ray data collection, which was monitored by recording of the crystal absorption spectra. Initially, the peroxo-anion species was formed and then protonated to yield compound O. Quantum chemical calculations indicate that the peroxo-anion species is not stable and collapses instantaneously to compound O. Compound O is present in the ferric low-spin doublet ground state and is characterized by a long O-O bond length of 1.5 angstrom and a Fe-O bond distance of 1.8 angstrom, which is also observed in the crystal structure.

引用

页码：99 / 104

页数：6

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