The molecular motion of bacteriorhodopsin mutant D96N in the purple membrane.
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.
Research Institute for Electronic Science, Hokkaido University, Sapporo, Japan.
T
T
Kikukawa
T
T
Araiso
K
K
Mukasa
T
T
Shimozawa
N
N
Kamo
D016880:Anisotropy; D001436:Bacteriorhodopsins / Q000235:genetics / Q000502:physiology* / Q000528:radiation effects; D006217:Halobacterium / Q000235:genetics; D008027:Light; D009038:Motion; D009154:Mutation; D018717:Purple Membrane / Q000502:physiology* / Q000528:radiation effects
D001436:Bacteriorhodopsins