Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate

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• 作者：Ken Okamoto ; Yuko Kawaguchi ; Bryan T. Eger ; Emil F. Pai ; Takeshi Nishino
• 刊名：Journal of the American Chemical Society
• 出版年：2010
• 出版时间：December 8, 2010
• 年：2010
• 卷：132
• 期：48
• 页码：17080-17083
• 全文大小：219K
• 年卷期：v.132,no.48(December 8, 2010)
• ISSN：1520-5126

文摘

Two contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 Å and of the reduced bovine milk enzyme at 2.1 Å, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine.