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

点击翻译按钮获取中文摘要

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.