Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.
Fluorescence and energy transfer of tryptophans in Aplysia myoglobin.
复制标题
海兔肌红蛋白中色氨酸的荧光和能量转移。
DOI：
10.1016/s0006-3495(87)83390-8
复制
发表时间：
1987
影响因子：
3.4
通讯作者：
Hochstrasser,RM
中科院分区：
文献类型：
--
作者：
Janes,SM;Holtom,G;Ascenzi,P;Brunori,M;Hochstrasser,RM
在10℃-15℃的水溶液中测量了apo和Met Limacina肌红蛋白和抹香鲸肌红蛋白中色氨酸残基的荧光衰减。在所有物种中，都观察到了多指数行为，其中单个组分表现出独特的频率相关发射特征。结果表明，所有MET样品中的色氨酸荧光都像从晶体几何结构预测的那样，被快速的Forster能量转移到血红素而猝灭。载脂蛋白的荧光类似于游离色氨酸溶液中的荧光。此外，还研究了在25℃至75℃温度范围内可逆热变性的荧光性质。
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.