Sensory and energy transduction: Light-activated retinal proteins
Sensory and energy transduction: Light-activated retinal proteins
复制标题
感觉和能量转导：光激活视网膜蛋白
作者：
L. Stryer
细菌视紫红质（BR），一种在盐细菌中发现的光驱动质子泵的发现，揭示了视网膜的光异构化具有超越其在高等生物视觉中的作用的意义1•最近在盐细菌中发现了另外两种光激活视网膜蛋白：盐细菌视紫红质（HR），作为氯离子泵，和感觉视紫红质（SR），这是趋光性受体。这些盐杆菌蛋白的遗传、化学、构象、光反应和调控在最近的研讨会上进行了探讨。通过将它们与视紫红质（脊椎动物视网膜杆状细胞中的光感受器蛋白）进行比较，丰富了对蛋白质的讨论。据报道，真核绿藻中的趋光受体和介导人类色觉的三种视锥色素促成了会议的生动活泼。细菌视紫红质视网膜群的横向位置已经通过含有氢化或特殊氘化视网膜的膜的中子衍射研究（NA Dench er, Berlin）。中子差图中的峰值与c端螺旋的位置非常吻合，其中包含赖氨酸216，残基通过质子化的希夫碱键连接到视网膜（R. Henderson, MRC Cambridge）。质子抽运光循环中去质子化的物质M412的x射线和电子衍射图与质子化的BR非常相似。结构变化的程度对应于一个或两个氨基酸残基移动约4a的距离。这些数据排除了整个螺旋的旋转或倾斜。细菌视紫红质视网膜基团中关键键的结构引起了人们的兴趣。共振拉曼光谱和固态13C-NMR提供了关于光循环过程中发色团精确结构变化的丰富信息。理论计算表明，在质子化状态下，Cl4-Cl5单键的旋转受到严重阻碍。这个单键被认为在非质子化状态和质子化状态下基本上是自由的，在席夫碱氮附近有一个负的反离子（K. Schulten, Munich）。Cl4-C15键的旋转可能是细菌视紫红质质子泵送的重要门控机制。傅里叶变换红外光谱表明，几种羧酸盐发生
THE discovery of bacteriorhodopsin (BR), a light-driven proton pump found in halobacteria, revealed that the photoisomerization of retinal has a significance extending beyond its role in vision in higher organisms 1• Two more light-activated retinal proteins have recently been identified in halobacteria: halorhodopsin (HR), which serves as a chloride ion pump, and sensory rhodopsin (SR), which is the receptor for phototaxis. The genetics, chemistry, conformation, photoreactions and regulation of these halobacterial proteins were explored at at recent workshop*. Discussion of the proteins was enriched by comparing them with rhodopsin, the photoreceptor protein in the rod cells of vertebrate retinas. Reports of a phototaxis receptor in a eucaryotic green alga 2 and the three cone pigments mediating human colour vision contributed to the liveliness of the meeting. The lateral position of the retinal group of bacteriorhodopsin has been investigated by neutron diffraction of membranes containing hydrogenated or specifically deuterated retinal (NA Dench er, Berlin). Peaks in neutron difference maps fit nicely with the proposed position of the C-terminal helix, which contains lysine 216, the residue joined to retinal by a protonated Schiff base linkage (R. Henderson, MRC Cambridge). X-ray and electron diffraction patterns of M412, the deprotonated species in the protonpumping photocycle, are very similar to those of protonated BR. The extent of structural change corresponds to a movement of one or two amino acid residues by a distance of about 4 A. A rotation or tilting of an entire helix is excluded by these data. The configurations of key bonds in the retinal group of bacteriorhodopsin attracted much interest. Resonance Raman spectroscopy and solid-state 13C-NMR have provided a wealth of information concerning the precise structural changes of the chromophore during the photocycle 3.4. Theoretical calculations indicate that rotation about the Cl4-Cl5 single bond is severely hindered in the protonated state. This single bond is thought to be essentially free in the unprotonated state, as well as in a protonated state, with a negative counter-ion near the Schiff base nitrogen (K. Schulten, Munich). Rotation about the Cl4-C15 bond may be an important gating mechanism in proton pumping by bacteriorhodopsin. Fourier transform infra-red spectroscopy has shown that several carboxylates undergo
DOI：
10.1073/pnas.79.20.6250
发表时间：
1982-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
--
作者：
BOGOMOLNI, RA;SPUDICH, JL
通讯作者：
SPUDICH, JL
控制跨膜离子通量以选择盐杆菌的盐视紫红质缺陷和其他能量转导突变体。
DOI：
10.1073/pnas.79.14.4308
发表时间：
1982
影响因子：
11.1
作者：
Spudich,EN;Spudich,JL
通讯作者：
Spudich,JL
DOI：
10.1073/pnas.81.6.1706
发表时间：
1984-01-01
期刊：
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子：
--
作者：
HARBISON, GS;SMITH, SO;GRIFFIN, RG
通讯作者：
GRIFFIN, RG