The interaction between apoCopC and cupric was investigated by fluorescence spectra, in phosphate (20 mmol/L) buffer at pH 6.0. Results suggest that the environ- ment is measured to be hydrophobic completely around tr...The interaction between apoCopC and cupric was investigated by fluorescence spectra, in phosphate (20 mmol/L) buffer at pH 6.0. Results suggest that the environ- ment is measured to be hydrophobic completely around tryptophan (83). At the same time, apoCopC fluorescence at 320 nm was significantly quenched with the addition of cu- pric and the 1:1 stoichiometric ratio of apoCopC to cupric was confirmed by fluorescence. In addition, the conditional binding constants were calculated to be KCu-Copc = (1.8±0.58)× 1013 mol?1 L on the basis of the results of fluorescence titra- tion curves. The apoCopC has the ability to bind specifically cupric ion.展开更多
基金supported by the National Natural Science Foundation of China(Grant No.20371031)the Natural Science Foundation of Shanxi Province(Grant No.20031017).
文摘The interaction between apoCopC and cupric was investigated by fluorescence spectra, in phosphate (20 mmol/L) buffer at pH 6.0. Results suggest that the environ- ment is measured to be hydrophobic completely around tryptophan (83). At the same time, apoCopC fluorescence at 320 nm was significantly quenched with the addition of cu- pric and the 1:1 stoichiometric ratio of apoCopC to cupric was confirmed by fluorescence. In addition, the conditional binding constants were calculated to be KCu-Copc = (1.8±0.58)× 1013 mol?1 L on the basis of the results of fluorescence titra- tion curves. The apoCopC has the ability to bind specifically cupric ion.
