Vanderkooi J M, Calhoun D B, Englander S W
Science. 1987 May 1;236(4801):568-9. doi: 10.1126/science.3576185.
A large number of proteins were tested for the property of intrinsic phosphorescence in deoxygenated aqueous solution at room temperature. The majority of proteins exhibit phosphorescence under normal solution conditions. Phosphorescence lifetimes from 0.5 millisecond to 2 seconds were observed in three-fourths of the proteins tested. The lifetime appears to correlate with relative isolation of the tryptophan indole side chain from solvent. With few exceptions, proteins in general can be expected to display a phosphorescence lifetime greater than 30 microseconds. This widespread characteristic of proteins has been largely overlooked because long-lived phosphorescence is highly sensitive to quenching by low levels of dissolved oxygen in solution. Protein phosphorescence offers a new time domain and a far wider dynamic range than has been used before for photoluminescence experimentation.
在室温下对大量蛋白质在脱氧水溶液中的固有磷光特性进行了测试。大多数蛋白质在正常溶液条件下会发出磷光。在四分之三的测试蛋白质中观察到了0.5毫秒至2秒的磷光寿命。该寿命似乎与色氨酸吲哚侧链与溶剂的相对隔离有关。除了少数例外，一般可以预期蛋白质的磷光寿命大于30微秒。蛋白质的这一广泛特性在很大程度上被忽视了，因为长寿命磷光对溶液中低水平溶解氧的猝灭非常敏感。蛋白质磷光提供了一个新的时域和比以前用于光致发光实验的动态范围宽得多的动态范围。
