儿茶酚氧化酶的晶体结构：对3型铜蛋白功能的新见解。
The crystal structure of catechol oxidase: new insight into the function of type-3 copper proteins.
作者信息
Gerdemann Carsten, Eicken Christoph, Krebs Bernt
机构信息
Institut für Anorganische und Analytische Chemie der Universität Münster, Wilhelm-Klemm-Strasse 8, 48149 Münster, Germany.
出版信息
Acc Chem Res. 2002 Mar;35(3):183-91. doi: 10.1021/ar990019a.
The crystal structure of catechol oxidase reveals new insight into the functional properties of the type-3 copper proteins. This class of proteins includes the closely related and better-known tyrosinase as well as hemocyanin, an oxygen transport protein. All these proteins have a dinuclear copper center, have similar spectroscopic behaviors, and show close evolutionary and functional relationships. Comparison between the 3D structures of catechol oxidase and hemocyanins reveals the structural reasons for the divergence in function.
儿茶酚氧化酶的晶体结构为3型铜蛋白的功能特性提供了新的见解。这类蛋白质包括密切相关且更为人熟知的酪氨酸酶以及作为氧运输蛋白的血蓝蛋白。所有这些蛋白质都有一个双核铜中心，具有相似的光谱行为，并显示出密切的进化和功能关系。儿茶酚氧化酶和血蓝蛋白的三维结构比较揭示了功能差异的结构原因。
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