Dér A, Száraz S, Tóth-Boconádi R, Tokaji Z, Keszthelyi L, Stoeckenius W
Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143.
Proc Natl Acad Sci U S A. 1991 Jun 1;88(11):4751-5. doi: 10.1073/pnas.88.11.4751.
Bacteriorhodopsin (bR568) in purple membrane near pH 2 shifts its absorption maximum from 568 to 605 nm forming the blue protein bRacid605, which no longer transports protons and which shows no transient deprotonation of the Schiff base upon illumination. Continued acid titration with HCl or HBr but not H2SO4 restores the purple chromophore to yield bRHCl564 or bRHBr568. These acid purple forms also regain transmembrane charge transport, but no transient Schiff base deprotonation is observed. In contrast to bR568, no rate decrease of the bRacidpurple transport kinetics is detected in 2H2O; however, the transport rate decreases by a factor of approximately 2 in bRHBr568 compared with bRHCl564. The data indicate that in the acid purple form bR transports the halide anions instead of protons. We present a testable model for the transport mechanism, which should also be applicable to halorhodopsin.
在接近pH 2的条件下,紫色膜中的细菌视紫红质(bR568)的最大吸收峰从568 nm移至605 nm,形成蓝色蛋白bRacid605,该蛋白不再转运质子,且在光照时席夫碱无瞬时去质子化现象。用HCl或HBr而非H2SO4继续进行酸滴定可使紫色发色团恢复,生成bRHCl564或bRHBr568。这些酸性紫色形式也恢复了跨膜电荷转运,但未观察到席夫碱的瞬时去质子化现象。与bR568不同,在2H2O中未检测到bRacid紫色形式的转运动力学速率降低;然而,与bRHCl564相比,bRHBr568中的转运速率降低了约2倍。数据表明,在酸性紫色形式中,bR转运卤化物阴离子而非质子。我们提出了一种可验证的转运机制模型,该模型也应适用于嗜盐视紫红质。