X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior

被引：34

作者：

McCormick, Michael S. ^{[1
]}

Sazinsky, Matthew H. ^{[1
]}

Condon, Karen L. ^{[1
]}

Lippard, Stephen J. ^{[1
]}

机构：

[1] MIT, Dept Chem, Cambridge, MA 02139 USA

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2006年 / 128卷 / 47期

关键词：

D O I：

10.1021/ja064837r

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

We report the X-ray crystal structures of native and manganese(II)-reconstituted toluene/o-xylene monooxygenase hydroxylase (ToMOH) from Pseudomonas stutzeri OX1 to 1.85 and 2.20 Å resolution, respectively. The structures reveal that reduction of the dimetallic active site is accompanied by a carboxylate shift and alteration of the coordination environment for dioxygen binding and activation. A rotamer shift in a strategically placed asparagine 202 accompanies dimetallic center reduction and is proposed to influence protein component interactions. This rotamer shift is conserved between ToMOH and the corresponding residue in methane monooxygenase hydroxylase (MMOH). Previously unidentified hydrophobic pockets similar to those present in MMOH are assigned. Copyright © 2006 American Chemical Society.

引用

页码：15108 / 15110

页数：3

共 33 条

[1] Reactions of the peroxo intermediate of soluble methane monooxygenase hydroxylase with ethers [J].