Kinetic and X-ray crystallographic analysis of quantum mechanical hydrogen tunneling in enzyme-catalyzed reaction

酶催化反应中量子力学氢隧道的动力学和X射线晶体学分析

• 批准号: 19770118
• 负责人: MURAKAWA Takeshi
• 金额: $ 2.49万
• 依托单位: Osaka Medical College
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Young Scientists (B)
• 财政年份: 2007
• 资助国家: 日本
• 起止时间: 2007 至 2009
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-19770118/
• 关键词: プロトントンネリング; ビルトインキノン補酵素; 同位体効果; ビルトイン補酵素; トパキノン

It is becoming widely accepted that the hydrogen tunneling is a general feature of the enzyme-catalyzed reaction at room temperature, especially in the reaction requiring high activation energy such as C-H bond cleavage. We analyzed stereospecific abstraction of substrate ・^-proton catalyzed by copper amine oxidases from Arthrobacter globiformis (AGAO) by transition-state kinetics and X-ray crystallographic analysis. These results provide new finding for enzyme-enhanced hydrogen tunneling.

氢隧穿是室温下酶催化反应的一个普遍特征，特别是在C-H键断裂等需要高活化能的反应中。利用过渡态动力学和X射线晶体学分析方法研究了球形节杆菌（Arthrobacter globiformis，AGAO）铜胺氧化酶催化底物·^-质子的立体专一性提取。这些结果为酶增强氢隧穿提供了新的发现。

项目成果

Further insight into the mechanism of streoselective proton abstraction by bacterial copper amine oxidase

进一步深入了解细菌铜胺氧化酶立体选择性质子夺取机制

• 发表时间: 2008
• 期刊: Biochemistry 47
• 作者: Masayasu Taki;Takeshi Murakawa (equally contributing);Takuya Nakamoto;Mayumi Uchida;Hideyuki Hayashi;Katsuyuki Tanizawa;Yukio Yamamoto;Toshihide Okajima
• 通讯作者: Toshihide Okajima

Acid-Base Chemistry in the Reductive Half-Reaction of Copper Amine Oxidase from Arthrobacter globiformis

球状节杆菌铜胺氧化酶还原半反应中的酸碱化学

• 发表时间: 2010