Key Laboratory of Pesticide & Chemical Biology (CCNU), Ministry of Education, College of Chemistry, Central China Normal University, Wuhan 430079, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2012 Apr;89:337-44. doi: 10.1016/j.saa.2011.12.014. Epub 2011 Dec 20.
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 Mg2+ or Mn2+ but cannot be activated by Ca2+ or Zn2+. Spectroscopic analysis of emission quenching showed that quenching mechanism of FBP/SBPase with Mg2+ or Mn2+ was static quenching mechanism while that of Ca2+ or Zn2+ was dynamic quenching process. Hydrogen bonds and van der Waals interaction might be the predominant intermolecular forces in stabilizing FBP/SBPase-Mg2+ while hydrophobic forces were the predominant intermolecular forces in stabilizing FBP/SBPase-Mn2+. 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.
果糖-1,6-/ 景天庚酮糖-1,7-二磷酸酶（FBP/SBPase）是寻找抑制剂以解决有害藻华的潜在重要靶标酶。在本文中，通过酶活性分析、荧光和分子建模方法研究了 FBP/SBPase 与金属离子的相互作用。酶活性分析表明，FBP/SBPase 可以被 Mg2+或 Mn2+激活，但不能被 Ca2+或 Zn2+激活。荧光猝灭的光谱分析表明，FBP/SBPase 与 Mg2+或 Mn2+的猝灭机制是静态猝灭机制，而与 Ca2+或 Zn2+的猝灭机制是动态猝灭过程。氢键和范德华相互作用可能是稳定 FBP/SBPase-Mg2+的主要分子间力，而疏水力是稳定 FBP/SBPase-Mn2+的主要分子间力。在结合反应中，FBP/SBPase 的微环境和构象发生了变化。还通过分子建模研究讨论了金属离子和重要氨基酸残基对 FBP/SBPase-金属离子复合物的影响。
