文献类型：期刊文献

英文题名：Inhibition of ferric ion to oxalate oxidase shed light on the substrate binding site

作者：Pang, Yu[1];Lan, Wanjun[1];Huang, Xuelei[1];Zuo, Guanke[1];Liu, Hui[1];Zhang, Jingyan[1]

机构：[1]E China Univ Sci & Technol, Sch Pharm, Shanghai Key Lab New Drug Design, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China

年份：2015

卷号：28

期号：5

起止页码：861

外文期刊名：BIOMETALS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000361430000006)】；

基金：This work was supported by the State key laboratory of bioreactor engineering (No. 2060204), NSFC of China (No. 20671034), and 111 Project (B07023).

语种：英文

外文关键词：Oxalate oxidase; Fe3+ ion; Inhibition; Computer modeling; Substrate binding site

摘要：Oxalate oxidase (OxOx), a well known enzyme catalyzes the cleavage of oxalate to carbon dioxide with reduction of dioxygen to hydrogen peroxide, however its catalytic process is not well understood. To define the substrate binding site, interaction of Fe3+ ions with OxOx was systemically investigated using biochemical method, circular dichrosim spectroscopy, microscale thermophoresis, and computer modeling. We demonstrated that Fe3+ is a non-competitive inhibitor with a milder binding affinity to OxOx, and the secondary structure of the OxOx was slightly altered upon its binding. On the basis of the structural properties of the OxOx and its interaction with Fe3+ ions, two residue clusters of OxOx were assigned as potential Fe3+ binding sites, the mechanism of the inhibition of Fe3+ was delineated. Importantly, the residues that interact with Fe3+ ions are involved in the substrate orienting based on computer docking. Consequently, the interaction of OxOx with Fe3+ highlights insight into substrate binding site in OxOx.