Bismuto E, Irace G, Colonna G, Jameson D M, Gratton E
Biochim Biophys Acta. 1987 Jun 17;913(2):150-4. doi: 10.1016/0167-4838(87)90324-4.
Dynamic aspects of the heme-binding site of myoglobins derived from two phylogenetically distant species, namely sperm whale and bluefin tuna, have been investigated by studying steady-state and time-resolved emission properties of 2-p-toluidinyl-6-naphthalene sulfonic acid (TNS) apomyoglobin conjugates. Multi-frequency phase and modulation fluorometry data indicate that charge movements occur in the fluorophore environment during the excited state lifetime in the sperm whale myoglobin system. In the case of the bluefin tuna myoglobin TNS adduct these movements were not detected, indicating that the relaxation processes differ in the two types of myoglobins.
通过研究2-对甲苯胺基-6-萘磺酸（TNS）与脱辅基肌红蛋白的缀合物的稳态和时间分辨发射特性，对来自两个系统发育距离较远的物种（抹香鲸和蓝鳍金枪鱼）的肌红蛋白血红素结合位点的动态方面进行了研究。多频相位和调制荧光测定数据表明，在抹香鲸肌红蛋白系统中，激发态寿命期间荧光团环境中发生了电荷移动。在蓝鳍金枪鱼肌红蛋白TNS加合物的情况下，未检测到这些移动，表明两种类型的肌红蛋白的弛豫过程不同。
