CAJ | 학술논문

利用紫外可见吸收光谱、荧光光谱、同步荧光光谱及圆二色(CD)光谱研究了铜(Ⅱ)离子与神经红蛋白(NGB)的相互作用.结果表明.Cu~(2+)离子使NGB在280 nm处的紫外吸收增强,说明Cu~(2+)与NGB发生了相互作用;Cu~(2+)使NGB内源性荧光发生猝灭,其猝灭机制为静态猝灭;同步荧光光谱表明,Cu~(2+)使色氨酸微环境的疏水性有所降低,Cu~(2+)对NGB的作用位点更接近于色氨酸;CD光谱显示Cu~(2+)没有引起NGB二级结构明显的变化.
이용자외가견흡수광보、형광광보、동보형광광보급원이색(CD)광보연구료동(Ⅱ)리자여신경홍단백(NGB)적상호작용.결과표명.Cu~(2+)리자사NGB재280 nm처적자외흡수증강,설명Cu~(2+)여NGB발생료상호작용;Cu~(2+)사NGB내원성형광발생졸멸,기졸멸궤제위정태졸멸;동보형광광보표명,Cu~(2+)사색안산미배경적소수성유소강저,Cu~(2+)대NGB적작용위점경접근우색안산;CD광보현시Cu~(2+)몰유인기NGB이급결구명현적변화.
The interaction of copper(Ⅱ) ion with Neuroglobin (NGB) was investigated by UV-Vis absorption spectra, fluorescence spectra, synchronous fluorescence spectra and circular dichroism (CD) spectra. The results show that Cu~(2+) can enhance the absorption intensity of NGB at 280 nm, intrinsic fluorescence of NGB is quenched with the addition of Cu~(2+), which belongs to static fluorescence quenching. The synchronous fluorescence spectra indicate the slight change of the microenvironment of tryptophan residues and that the binding site is closer to tryptophan than tyrosine residues. The secondary structure of NGB has no obvious change with the addition of Cu~(2+) as shown in CD spectra.