Spectroscopic study on the interaction of catalase with bifendate and analogs
作者： Ruiqiang Wang , Lu Zhang , Rui Wang , Huanjing Dou , Hua Li
DOI: 10.1016/J.SAA.2012.10.039
关键词: Catalase 、 Synchronous fluorescence 、 Residue (chemistry) 、 Quenching (fluorescence) 、 Intrinsic fluorescence 、 Fluorescence spectra 、 Absorption (chemistry) 、 Photochemistry 、 Chemistry
摘要: Abstract The interactions of bifendate (DDB) or analogs (Bicyclol, I, II and III) with catalase are analyzed by spectrophotometric methods. fluorescence spectra results show the intrinsic is strongly quenched DDB a static quenching procedure. binding constants obtained at three temperatures. thermodynamics parameters (ΔH, ΔS, ΔG) indicate hydrophobic electrostatic play major role in interaction. synchronous fluorescence, UV–vis absorption three-dimensional demonstrate that microenvironments Trp residue disturbed analogs. Thermodynamic showed strongest quencher bind to highest affinity among five compounds.
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