Copper amine oxidase: cunning cofactor and controversial copper

被引：49

作者：

Dawkes, HC ^{[1
]}

Phillips, SEV ^{[1
]}

机构：

[1] Univ Leeds, Sch Biochem & Mol Biol, Astbury Ctr Struct Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2001年 / 11卷 / 06期

关键词：

D O I：

10.1016/S0959-440X(01)00270-6

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：

Copper amine oxidases have a complex reaction cycle that converts a primary amine and molecular oxygen into the aldehyde, ammonia and hydrogen peroxide. Coupling structural studies of freeze-trapped reaction intermediates in crystals with kinetic and spectroscopic experiments in solution has generated a detailed molecular picture of catalysis. Although dioxygen has been directly observed bound to the copper at a late stage in the reaction cycle, whether copper is the initial binding site remains controversial.

引用

页码：666 / 673

页数：8

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