报告题目：酶催化氧化反应
报告人：Prof. Aimin Liu
报告时间：2014年11月11日（星期二）下午2:00
报告地点：必威西汉姆联官网中北校区化学馆A205报告厅
报告人简介：
1997‐1999, Ph.D., Biophysics, Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University,
Stockholm, Sweden.
1986‐1991, 博士, 中国科学院兰州化学物理研究所.
1981‐1986, 学士, 中国科技大学.
1997‐1999, 厦门大学副教授.
08/200‐07/2012, Associate Professor of Chemistry and Biochemistry, Department Of Chemistry, Georgia State University, Atlanta, GA.
08/2012‐present, Professor of Chemistry and Biochemistry with tenure, Department of Chemistry, Georgia State University, Atlanta, GA.
报告内容：
The MauG-catalyzed reaction is a three-step, six-electron oxidation process. Each step requires one equivalent of H2O2 as the oxidant.We have previously shown that an unprecedented high-valence bis-Fe(IV) intermediate of MauG orchestrates the oxidative production of TTQ.From our most recent EPR study, a novel tryptophan-based di-radical intermediate has been captured in the substrate protein preMADH as a result of oxidation by the bis-Fe(IV) species. In this presentation, I will focus on the long-range remote enzyme catalysis mechanism of TTQ biosynthesis with particular emphases on the chemical properties of these two critical intermediates.