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与脱辅基肌红蛋白结合的荧光探针的纳秒级衰变研究。

Nanosecond decay studies of a fluorescence probe bound to apomyoglobin.

作者信息

Gafni A, DeToma R P, Manrow R E, Brand L

出版信息

Biophys J. 1977 Feb;17(2):155-68. doi: 10.1016/S0006-3495(77)85633-6.

Abstract

Excited state interactions of N-(p-tolyl)-2-aminonaphthalene-6-sulfonate (2, 6 p-TNS) bound to apomyoglobin were studied by nanosecond time-resolved emission spectroscopy. A dynamic interaction of the excited dye molecule with its binding site, associated with a significant change in the emission energy with time, was observed. The decay kinetics were found to be complex and consistent with the kinetic model for solvent relaxation as proposed by Bakhshiev et al. (Opt. Spectrosc. 21:307. 1966). The behavior of 2, 6 p-TNS bound to apomyoglobin was found to be qualitatively similar to that of the dye dissolved in a viscous solvent such as glycerol or adsorbed to egg lecithin vesicles. The detailed information obtained by following the changes in emission spectra of fluorescent probes on the nanosecond time scale leads to a better understanding of their interactions with biological systems.

摘要

通过纳秒时间分辨发射光谱研究了与脱辅基肌红蛋白结合的N-(对甲苯基)-2-氨基萘-6-磺酸盐(2,6 p-TNS)的激发态相互作用。观察到激发态染料分子与其结合位点的动态相互作用,这与发射能量随时间的显著变化有关。发现衰减动力学很复杂,并且与Bakhshiev等人(《光学光谱学》21:307. 1966)提出的溶剂弛豫动力学模型一致。发现与脱辅基肌红蛋白结合的2,6 p-TNS的行为在定性上类似于溶解在甘油等粘性溶剂中或吸附在卵磷脂囊泡上的染料的行为。通过在纳秒时间尺度上跟踪荧光探针发射光谱的变化获得的详细信息,有助于更好地理解它们与生物系统的相互作用。

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本文引用的文献

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Fluorescence probes for structure.用于结构的荧光探针。
Annu Rev Biochem. 1972;41:843-68. doi: 10.1146/annurev.bi.41.070172.004211.

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