漆酶
化学
氧化酶试验
结晶学
过氧化物酶
配体(生物化学)
细胞色素c氧化酶
氧化还原酶
金属蛋白
多铜氧化酶
晶体结构
氧化还原
二聚体
协调球
铜
立体化学
活动站点
酶
生物化学
无机化学
有机化学
受体
作者
Valérie M.-A. Ducros,Andrzej M. Brzozowski,Keith T. Wilson,Stephen J. Brown,Peter Rahbek Østergaard,Palle Schneider,Debbie Yaver,Anders Gorm Pedersen,Gideon J. Davies
摘要
Laccase catalyses the oxidation of a variety of organic substrates coupled to the reduction of oxygen to water. It is widely believed to be the simplest representative of the ubiquitous blue multi-copper oxidase family. Laccase is implicated in a wide spectrum of biological activities and, in particular, plays a key role in morphogenesis, development and lignin metabolism in fungi and plants. The structure of laccase from the fungus Coprinus cinereus has been determined by X-ray crystallography at a resolution of 2.2 A. Laccase is a monomer composed of three cupredoxin-like beta-sandwich domains, similar to that found in ascorbate oxidase. In contrast to ascorbate oxidase, however, the mononuclear type-1 Cu site lacks the axial methionine ligand and so exhibits trigonal planar coordination, consistent with its elevated redox potential. Crucially, the structure is trapped in a Cu depleted form in which the putative type-2 Cu atom is completely absent, but in which the remaining type-1 and type-3 Cu sites display full occupancy. Type-2 Cu depletion has unexpected consequences for the coordination of the remaining type-3 Cu atoms.
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