Add time:08/14/2019         Source:sciencedirect.com

The interaction between pyridoxal hydrochloride (HQ) and apoCopC was investigated using Fourier transform infrared spectroscopy (FTIR), isothermal titration calorimetry (ITC), circular dichroism (CD), fluorescence spectroscopy, three-dimensional (3D) fluorescence spectroscopy, fluorescence lifetime, TNS fluorescence and docking methods. FTIR, CD, TNS fluorescence and fluorescence lifetime experiments suggested that the apoCopC conformation was altered by HQ with an increase in the random coil content and a reduction in the β-sheet content. In addition, the data from fluorescence spectroscopy, 3D fluorescence spectroscopy and molecular docking revealed that the binding site of HQ was located in the hydrophobic area of apoCopC, and a redshift of the HQ fluorescence spectra was observed. Furthermore, ITC and fluorescence quenching data manifested that the binding ratio of HQ and apoCopC was 1:1, and the forming constant was calculated to be (7.06 ± 0.21) × 105 M−1. The thermodynamic parameters ΔH and ΔS suggested that the formation of a CopC-HQ complex depended on the hydrophobic force. Furthermore, the average binding distance between tryptophan in apoCopC and HQ was determined by means of Förster non-radioactive resonance energy transfer and molecular docking. The results agreed well with each other. As a redox switch in the modulation of copper, the interaction of apoCopC with small molecules will affect the action of the redox switch. These findings could provide useful information to illustrate the copper regulation mechanism.

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