title: Spectroscopic study on the interaction of catalase with bifendate and analogs.
abstract: The interactions of bifendate (DDB) or analogs (Bicyclol, I, II and III) with catalase are analyzed by spectrophotometric methods. The fluorescence spectra results show the intrinsic fluorescence of catalase is strongly quenched by DDB or analogs with a static quenching procedure. The binding constants are obtained at three temperatures. The thermodynamics parameters (ΔH, ΔS, ΔG) indicate the hydrophobic and electrostatic interactions play a major role in the interaction. The results of synchronous fluorescence, UV-vis absorption and three-dimensional fluorescence spectra demonstrate that the microenvironments of Trp residue of catalase are disturbed by the analogs. Thermodynamic results showed that DDB is the strongest quencher and bind to catalase with the highest affinity among five compounds.
authors.affiliation: The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China.
authors.forename: Ruiqiang
authors.initials: R
authors.lastname: Wang
authors.forename: Lu
authors.initials: L
authors.lastname: Zhang
authors.forename: Rui
authors.initials: R
authors.lastname: Wang
authors.forename: Huanjing
authors.initials: H
authors.lastname: Dou
authors.forename: Hua
authors.initials: H
authors.lastname: Li
authors.forename: Yi
authors.initials: Y
authors.lastname: Wang
authors.forename: Juanjuan
authors.initials: J
authors.lastname: Pu
authors.forename: Ruiyong
authors.initials: R
authors.lastname: Wang
mesh_terms: D000818:Animals; D000998:Antiviral Agents / Q000737:chemistry / Q000494:pharmacology*; D001665:Binding Sites; D001713:Biphenyl Compounds / Q000737:chemistry / Q000494:pharmacology*; D002374:Catalase / Q000378:metabolism*; D002417:Cattle; D006505:Hepatitis / Q000188:drug therapy; D008099:Liver / Q000201:enzymology*; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics
chemical_list: D000998:Antiviral Agents; D001713:Biphenyl Compounds; C465548:bifendate; C477843:bicyclol; D002374:Catalase