Calculated and Experimental Spin State of Seleno Cytochrome P450

被引：25

作者：

Jiang, Yongying ^{[1
]}

Sivaramakrishnan, Santhosh ^{[1
]}

Hayashi, Takahiro ^{[2
]}

Cohen, Shimrit ^{[3
,4
]}

Moenne-Loccoz, Pierre ^{[2
]}

Shaik, Sason ^{[3
,4
]}

de Montellano, Patti R. Ortiz ^{[1
]}

机构：

[1] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94158 USA

[2] Oregon Hlth & Sci Univ, Dept Sci & Engn, Beaverton, OR 97006 USA

[3] Hebrew Univ Jerusalem, Inst Chem, IL-91904 Jerusalem, Israel

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

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2009年 / 48卷 / 39期

关键词：

cytochrome P450; proteins; Raman spectroscopy; selenium; spin states; CLUSTER COMPLEXES; NADPH OXIDASE; ACTIVE-SITE; SELENOCYSTEINE; P450(CAM); P450CAM; LIGAND; MUTANT; SE; CYSTEINE-436;

D O I：

10.1002/anie.200901485

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A change for the better: The proximal cysteine thiolate in a cytochrome P450 enzyme is replaced by a selenocysteine. The resulting selenolate-ligated CYP119 protein has UV/Vis (see spectrum, ), EPR, and resonance Raman spectra that are similar to those of the native protein ( - ). These results are the first to fully describe a hemoprotein with a selenolate proximal ligand. © 2009 Wiley-VCH Verlag GmbH & Co. KCaA.

引用

页码：7193 / 7195

页数：3

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