Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature.
Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature.
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DOI：
10.1073/pnas.83.2.347
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发表时间：
1986
影响因子：
11.1
通讯作者：
K. Rothschild;P. Roepe;P. Ahl;T. Earnest;R. Bogomolni;S. K. Gupta;C. M. Mulliken;J. Herzfeld
中科院分区：
文献类型：
--
作者：
K. Rothschild;P. Roepe;P. Ahl;T. Earnest;R. Bogomolni;S. K. Gupta;C. M. Mulliken;J. Herzfeld
同位素标记的酪氨酸已选择性地掺入细菌紫红质（BR）中。这些样品和正常BR的低温BR570与K傅立叶变换红外差异光谱的比较提供了有关酪氨酸在一级光传输中的作用的信息。发现了一些酪氨酸对差异谱的贡献。这些结果和与模型化合物光谱的比较表明，在BR570到K转变期间硫化基团质子化。紫外线差异光谱法的结果得到了强烈支持。
Isotopically labeled tyrosines have been selectively incorporated into bacteriorhodopsin (bR). A comparison of the low-temperature bR570 to K Fourier transform infrared-difference spectra of these samples and normal bR provides information about the role of tyrosine in the primary phototransition. Several tyrosine contributions to the difference spectrum are found. These results and comparison with the spectra of model compounds suggest that a tyrosinate group protonates during the bR570 to K transition. This conclusion is strongly supported by the results of UV difference spectroscopy.