Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins

被引：41

作者：

Do, Loi H. ^{[2
]}

Hayashi, Takahiro ^{[1
]}

Moenne-Loccoz, Pierre ^{[1
]}

Lippard, Stephen J. ^{[2
]}

机构：

[1] Oregon Hlth & Sci Univ, Sch Med, Dept Sci & Engn, Beaverton, OR 97006 USA

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

来源：

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY | 2010年 / 132卷 / 04期

关键词：

NONHEME IRON ENZYMES; DIOXYGEN ACTIVATION; RIBONUCLEOTIDE REDUCTASE; OXYGEN ACTIVATION; O-2; ACTIVATION; HYDROXYLASE; COORDINATION; FREQUENCIES; CENTERS; BOND;

D O I：

10.1021/ja909718f

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Addition of H+ to a synthetic (mu-1,2-peroxo)diiron(III) model complex results in protonation of a carboxylate rather than the peroxo ligand. This conclusion is based on spectroscopic evidence from UV-vis, Fe-57 M-0 ssbauer. resonance Raman. infrared, and H-1/F-19 NMR Studies. These results Suggest a similar role for protons in the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged diiron enzymes.

引用

页码：1273 / +

页数：5

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