Kikukawa T, Araiso T, Mukasa K, Shimozawa T, Kamo N
Research Institute for Electronic Science, Hokkaido University, Sapporo, Japan.
FEBS Lett. 1995 Dec 27;377(3):502-4. doi: 10.1016/0014-5793(95)01408-X.
We measured the flash-induced absorption anisotropies of mutant bacteriorhodopsin (bR), D96N, in the purple membrane suspension. The measured anisotropy decay at 410 nm differed from that at 570 nm. These wavelength-dependent anisotropies show that the motion of absorption dipole of non-excited bR is faster than that of M-intermediate. The motion of non-excited bR is considered as the rotational motion of whole protein in the purple membrane. This fact suggests that the photo-excitation induces the conformational change of the protein and/or the inter-protein interaction within the membrane, which prevents the motion of M-intermediate.
我们测量了紫色膜悬浮液中突变型细菌视紫红质（bR）D96N的闪光诱导吸收各向异性。在410nm处测得的各向异性衰减与在570nm处不同。这些波长依赖性各向异性表明，未激发的bR吸收偶极子的运动比M中间体的运动更快。未激发的bR的运动被认为是紫色膜中整个蛋白质的旋转运动。这一事实表明，光激发诱导了蛋白质的构象变化和/或膜内蛋白质间的相互作用，从而阻止了M中间体的运动。
