Dencher N A, Dresselhaus D, Zaccai G, Büldt G
Department of Physics/Biophysics, Freie Universität Berlin, Federal Republic of Germany.
Proc Natl Acad Sci U S A. 1989 Oct;86(20):7876-9. doi: 10.1073/pnas.86.20.7876.
A neutron diffraction study of spectroscopic states for the light-energized proton pump bacteriorhodopsin (BR) is presented. The photocycle states BR-568 and M were generated at temperatures above 4 degrees C and were measured after trapping at--180 degrees C. In the BR-568 to M-state transition, which is known to be a key step in transmembrane proton pumping, reversible structural changes of the protein were detected. These structural alterations occur in the neighborhood of the cyclohexene ring and at the Schiff's base end of the chromophore retinal. They are interpreted as a 1-2 degree tilt of three or four of the transmembrane alpha-helices or as positional changes of four or five amino acids. The structural changes observed are inherent in the transport mechanism of bacteriorhodopsin.
本文介绍了对光激发质子泵细菌视紫红质(BR)光谱状态的中子衍射研究。光循环状态BR - 568和M在4摄氏度以上的温度下产生,并在捕获于零下180摄氏度后进行测量。在BR - 568到M状态的转变中,这是已知的跨膜质子泵浦的关键步骤,检测到了蛋白质的可逆结构变化。这些结构改变发生在环己烯环附近以及发色团视黄醛的席夫碱末端。它们被解释为三到四个跨膜α - 螺旋倾斜1 - 2度或四到五个氨基酸的位置变化。观察到的结构变化是细菌视紫红质转运机制所固有的。