Abstract
The interaction of benzidine (BZ) with hemocyanin (Hc) from Chinese mitten crab ( Eriocheir japonica sinensis) was studied by fluorescence spectrum. BZ can quench the fluorescence of Hc by forming a new complex. The process of binding BZ on Hc was a spontaneous molecular interaction procedure. The thermodynamic parameters, the enthalpy change and entropy change were estimated to be 47.36 kJ mol −1, 248.51 J mol −1 K −1 according to the van’ Hoff equation. This indicates that hydrophobic interaction played a major role in stabilizing the complex. The results of synchronous fluorescence spectroscopy and three-dimensional fluorescence spectra indicated that the structure of these tyrosine residues environments was altered by BZ, which could enter into the hydrophobic pocked of Hc.
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