Mechanistic Investigation of Oxygen Rebound in a Mononuclear Nonheme Iron Complex

被引：18

作者：

Pangia, Thomas M. ^{[1
]}

Yadav, Vishal ^{[1
]}

Gerard, Emilie F. ^{[2
,3
]}

Lin, Yen-Ting ^{[2
,3
]}

de Visser, Sam P. ^{[2
,3
]}

Jameson, Guy N. L. ^{[4
]}

Goldberg, David P. ^{[1
]}

机构：

[1] Johns Hopkins Univ, Dept Chem, 3400 North Charles St, Baltimore, MD 21218 USA

[2] Univ Manchester, Manchester Inst Biotechnol, 131 Princess St, Manchester M1 7DN, Lancs, England

[3] Univ Manchester, Sch Chem Engn & Analyt Sci, 131 Princess St, Manchester M1 7DN, Lancs, England

[4] Univ Melbourne, Mol Sci & Biotechnol Inst Bio21, Sch Chem, 30 Flemington Rd, Parkville, Vic 3010, Australia

来源：

INORGANIC CHEMISTRY | 2019年 / 58卷 / 15期

基金：

英国生物技术与生命科学研究理事会;

关键词：

KETOGLUTARATE DIOXYGENASE TAUD; C-H HYDROXYLATION; ALIPHATIC HALOGENASE; OXIDATION; REACTIVITY; PHENOLS; CYTOCHROME-P450; IRON(IV)-OXO; INSIGHTS; TAURINE;

D O I：

10.1021/acs.inorgchem.9b01208

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

An iron(III) methoxide complex reacts with para-substituted triarylmethyl radicals to give iron(II) and methoxyether products. Second-order rate constants for the radical derivatives were obtained. Hammett and Marcus plots suggest the radical transfer reactions proceed via a concerted process. Calculations support the concerted nature of these reactions involving a single transition state with no initial charge transfer. These findings have implications for the radical "rebound" step invoked in nonheme iron oxygenases, halogenases, and related synthetic catalysts.

引用

页码：9557 / 9561

页数：5

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