An Artificial Oxygenase Built from Scratch: Substrate Binding Site Identified Using a Docking Approach

被引：41

作者：

Esmieu, Charlene ^{[1
]}

Cherrier, Mickael V. ^{[2
]}

Amara, Patricia ^{[2
]}

Girgenti, Elodie ^{[1
]}

Marchi-Delapierre, Caroline ^{[1
]}

Oddon, Frederic ^{[1
]}

Iannello, Marina ^{[2
]}

Jorge-Robin, Adeline ^{[1
]}

Cavazza, Christine ^{[2
]}

Menage, Stephane ^{[1
]}

机构：

[1] Univ Grenoble 1, CNRS, CEA, DSV,iRTSV,UMR5249,LCBM, F-38041 Grenoble, France

[2] Univ Grenoble 1, CNRS, CEA,Metalloprot Unit, Inst Biol Struct Jean Pierre Ebel,UMR 5075, F-38027 Grenoble 1, France

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2013年 / 52卷 / 14期

关键词：

computational chemistry; iron; metalloenzymes; oxidation; sulfur; MANGANESE COMPLEXES; CIS-DIHYDROXYLATION; HYBRID CATALYST; METALLOENZYMES; DESIGN; OXIDATION; IRON; METALLOPROTEINS; EPOXIDATION; OLEFINS;

D O I：

10.1002/anie.201209021

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The substrate for an artificial iron monooxygenase was selected by using docking calculations. The high catalytic efficiency of the reported enzyme for sulfide oxidation was directly correlated to the predicted substrate binding mode in the protein cavity, thus illustrating the synergetic effect of the substrate binding site, protein scaffold, and catalytic site. © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

引用

页码：3922 / 3925

页数：4

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