Multicopper oxidases: intramolecular electron transfer and O2 reduction

被引：27

作者：

Wherland, Scot ^{[1
]}

Farver, Ole ^{[2
]}

Pecht, Israel ^{[3
]}

机构：

[1] Washington State Univ, Dept Chem, Pullman, WA 99164 USA

[2] Univ Copenhagen, Dept Analyt & Bioinorgan Chem, DK-2100 Copenhagen O, Denmark

[3] Weizmann Inst Sci, Dept Immunol, IL-76100 Rehovot, Israel

来源：

JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY | 2014年 / 19卷 / 4-5期

关键词：

Oxidases; Copper proteins; Electron transfer; Metalloprotein; Oxygen; RHUS-VERNICIFERA LACCASE; TRINUCLEAR COPPER CLUSTER; ENZYME ASCORBATE OXIDASE; CRYSTAL-STRUCTURE; STREPTOMYCES-COELICOLOR; HUMAN CERULOPLASMIN; DIOXYGEN REDUCTION; PEROXIDE BINDING; BLUE-PROTEINS; COTA-LACCASE;

D O I：

10.1007/s00775-013-1080-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The multicopper oxidases are an intriguing, widespread family of enzymes that catalyze the reduction of O-2 to water by a variety of single-electron and multiple-electron reducing agents. The structure and properties of the copper binding sites responsible for the latter chemical transformations have been studied for over 40 years and a detailed picture is emerging. This review focuses particularly on the kinetics of internal electron transfer between the type 1 (blue) copper site and the trinuclear center, as well as on the nature of the intermediates formed in the oxygen reduction process.

引用

页码：541 / 554

页数：14

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