| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1404175 | Journal of Molecular Structure | 2008 | 5 Pages |
The interaction of pazufloxacin mesilate (PZFX) with catalase was studied by spectroscopic methods under simulative physiological conditions. It was observed that the PZFX quenched the intrinsic fluorescence of catalase through a static quenching procedure. Gradual addition of catalase led to a marked increase in fluorescence anisotropy (r), it was suggested that the drug was located in a restricted environment of catalase. The negative ΔH0 and ΔS0 values in the case of PZFX with catalase complex implied that both hydrogen bonds and electrostatic interactions might play a significant role in PZFX binding to catalase. Circular dichorism (CD) spectra detection supported a change in the secondary structure of protein caused by the interaction of PZFX with catalase.
