Study on the interaction between cyanobacteria FBP/SBPase and metal ions

文献类型: 外文期刊

第一作者: Sun, Yao

作者: Sun, Yao;Liao, Xun;Li, Ding;Feng, Lingling;Wang, Xiaofeng;Jin, Jing;Yi, Fan;Zhou, Li;Wan, Jian;Li, Jun

作者机构:

关键词: Fluorescence;Fructose-1;6-/sedoheptulose-1;7-bisphosphatase;Interaction;Metal ion;Molecular modeling

期刊名称:SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY ( 影响因子:4.098; 五年影响因子:3.464 )

ISSN:

年卷期:

页码:

收录情况: SCI

摘要: Fructose-1,6-/sedoheptulose-1,7-bisphosphatase (FBP/SBPase) is a potential important target enzyme for finding inhibitors to solve harmful algal bloom. In this paper, the interactions between FBP/SBPase and metal ions were studied by enzyme activity analysis, fluorescence and molecular modeling method. The enzyme activity analysis showed that FBP/SBPase can be activated by Mg ~(2+) or Mn ~(2+) but cannot be activated by Ca ~(2+) or Zn ~(2+). Spectroscopic analysis of emission quenching showed that quenching mechanism of FBP/SBPase with Mg 2+ or Mn 2+ was static quenching mechanism while that of Ca ~(2+) or Zn ~(2+) was dynamic quenching process. Hydrogen bonds and van der Waals interaction might be the predominant intermolecular forces in stabilizing FBP/SBPase-Mg ~(2+) while hydrophobic forces were the predominant intermolecular forces in stabilizing FBP/SBPase-Mn ~(2+). Microenvironment and conformation of FBP/SBPase were changed in binding reaction. The effect of metal ions and important amino acid residues on FBP/SBPase-metal ion complex was also discussed by molecular modeling study.

分类号: O657.3

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