细菌视紫红质L中间体中的色氨酸扰动：基于吲哚-15N位移的傅里叶变换红外分析
Tryptophan perturbation in the L intermediate of bacteriorhodopsin: fourier transform infrared analysis with indole-15N shift.
作者信息
Maeda A, Sasaki J, Ohkita Y J, Simpson M, Herzfeld J
机构信息
Department of Biophysics, Faculty of Science, Kyoto University, Japan.
出版信息
Biochemistry. 1992 Dec 22;31(50):12543-5. doi: 10.1021/bi00165a001.
In the photoreaction of bacteriorhodopsin, the L intermediate shows an intense band at 3486 cm-1 which is unaffected by 2H2O (Maeda, A., Sasaki, J., Shichida, Y., & Yoshizawa, T. (1992) Biochemistry 31, 462-467]. This band is shifted to 3477 cm-1 by [indole-15N]tryptophan substitution and therefore is assigned to the N-H stretching vibration of the indole of tryptophan. Free indole in carbon tetrachloride shows its N-H stretching vibration at 3491 cm-1 [Fuson, N., Josien, M.-L., Powell, R. L., & Utterback, E. (1952) J. Chem. Phys. 20, 145-152]. Thus, it is suggested that at least one tryptophan residue in the L intermediate is not hydrogen bonded.
在细菌视紫红质的光反应中，L中间体在3486 cm-1处显示出一条强带，该带不受2H2O的影响（前田，A.，佐佐木，J.，志田，Y.，&吉泽，T.（1992年）《生物化学》31卷，462 - 467页）。这条带通过[吲哚-15N]色氨酸取代移至3477 cm-1，因此被归属于色氨酸吲哚的N - H伸缩振动。四氯化碳中的游离吲哚在3491 cm-1处显示其N - H伸缩振动[富森，N.，乔西安，M.-L.，鲍威尔，R. L.，&厄特巴克，E.（1952年）《化学物理杂志》20卷，145 - 152页]。因此，有人提出L中间体中至少有一个色氨酸残基没有形成氢键。
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