Cooperativity-regulated parallel pathways of the bacteriorhodopsin photocycle.
The paper demonstrates that the actinic light density dependence of the millisecond part of the bacteriorhodopsin (BR) photocycle at high pH predicts a model, which is the same in the sequence of the intermediates as concluded previously on the basis of double flash experiments [1992, FEBS Lett. 311, 267-270]. This model consists of the Mf-->N-->BR and M(s)-->BR parallel pathways, the relative yields of which are regulated by cooperative interaction of the BR molecules. The decay of M(s) is always slower than the decay of Mf and described as a direct reprotonation of the Schiff-base from the bulk, and the recovery of the ground-state nearly at the same time. M(s) is decomposed into M'f and M's. The first does not reprotonate, and similarly to Mf, it is suggested to be before the conformational change (switch), which latter process would be just before the decay of Mf. A simple way for the determination of the kinetics is also used. This confirms that the amount of N decreases with increasing fraction cycling and shows that the decay rate of N is independent of the fraction cycling. The differences in the kinetics are compared to each other, and they seem to allow a new way of kinetic evaluation at least under special conditions. The aim of this paper was briefly explained in my poster presented on the VIth International Conference on Retinal Protein (see [14]).
Tokaji
Z
Z
Institute of Biophysics, Hungarian Academy of Sciences, Szeged.
D001436:Bacteriorhodopsins / Q000737:chemistry* / Q000528:radiation effects; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008027:Light; D008956:Models, Chemical; D011522:Protons
D011522:Protons; D001436:Bacteriorhodopsins