Abstract：

Cytochrome P450 monooxygenase are a superfamily of heme enzyme with a cysteine as axial ligand, which catalyze the monooxygenation of various organic substrates under mild conditions. P450s are synthetically useful enzymes and promising versatile oxidative biocatalysts. However, the practical use of P450 is limited by its co-enzyme NAD(P)H and complexed electron transport system. Using H2O2 can simple the catalytic cycle of P450, however, most of P450s are inactive in the presence of H2O2. To overcome the problem, by mimicking the molecular structure and catalytic mechanism of natural peroxygenase and peroxidase, we have recently constructed an artificial P450 peroxygenase system with the assistance of dual-functional small molecule (DFSM) for the first time, which provides an alternative approach for the activation of the normally H2O2-inert P450BM3 enzyme. In combination with protein engineering, the DFSM-facilitated P450 peroxygenase system has been employed to the various oxidation reactions of non-native substrates, such as alkanes epoxidation, sulfoxidation of thioanisole, alkanes and aromatic hydroxylation, and so on, which showed unique activities, regio- and enantioselectivities in comparison with the natural P450 enzyme.

报告人简介：

丛志奇, 博士、研究员、博士生导师，中国科学院青岛生物能源与过程研究所，单碳酶催化研究组组长。于2009年在日本熊本大学获得理学博士学位，随后在日本分子科学研究所和名古屋大学从事博士后研究，参与多项日本文部省基础和重大研究课题。2016年回国工作后主持国家自然科学基金面上项目2项、青岛市创新领军人才计划、青岛能源所十三五期间“一三五”重点培育方向项目等研究课题。以第一和通讯作者在J Am Chem Soc、Angew Chem Int Ed、ACS Catal等国际期刊发表研究论文20多篇。主要研究方向是金属酶的化学机理解析、生物酶催化及其在合成生物技术上的应用。相关研究成果被ChemistryViews、中国科学报、中科院网站、基金委网站等专题报道，并被权威学术杂志多次正面引用和评述。