Janes S M, Holtom G, Ascenzi P, Brunori M, Hochstrasser R M
Biophys J. 1987 Apr;51(4):653-60. doi: 10.1016/S0006-3495(87)83390-8.
The fluorescence decay of tryptophan residues in apo and met Aplysia limacina myoglobin and sperm whale myoglobin were measured in aqueous solution at 10 degrees-15 degrees C. In all species, multiexponential behavior was observed in which the individual components displayed unique frequency-dependent emission characteristics. The results suggest that the tryptophan fluorescence in all met samples are quenched by rapid Forster energy transfer to the heme as predicted from the crystal geometry. Fluorescence from the apo protein is similar to that in solutions of free tryptophans. In addition, the fluorescence properties of the reversible thermal denaturation of Aplysia limacina met myoglobin was investigated between 25 degrees and 75 degrees C.
在10摄氏度至15摄氏度的水溶液中，测量了脱辅基和高铁的海兔肌红蛋白以及抹香鲸肌红蛋白中色氨酸残基的荧光衰减。在所有物种中，均观察到多指数行为，其中各个组分表现出独特的频率依赖性发射特性。结果表明，如根据晶体几何结构所预测的那样，所有高铁样品中的色氨酸荧光通过快速的福斯特能量转移至血红素而被淬灭。脱辅基蛋白的荧光与游离色氨酸溶液中的荧光相似。此外，还研究了在25摄氏度至75摄氏度之间海兔高铁肌红蛋白可逆热变性的荧光特性。
