Chemical and physical evidence for multiple functional steps comprising the M state of the bacteriorhodopsin photocycle.
In the photocycle of bacteriorhodopsin (bR), light-induced transfer of a proton from the Schiff base to an acceptor group located in the extracellular half of the protein, followed by reprotonation from the cytoplasmic side, are key steps in vectorial proton pumping. Between the deprotonation and reprotonation events, bR is in the M state. Diverse experiments undertaken to characterize the M state support a model in which the M state is not a static entity, but rather a progression of two or more functional substates. Structural changes occurring in the M state and in the entire photocycle of wild-type bR can be understood in the context of a model which reconciles the chloride ion-pumping phenotype of mutants D85S and D85T with the fact that bR creates a transmembrane proton-motive force.
Betancourt
F M
FM
Life Sciences Division, Donner Laboratory, Lawrence Berkeley, National Laboratory, University of California, Berkeley, CA 94720, USA. fmh@xtalu.lbl.gov
Glaeser
R M
RM
D001436:Bacteriorhodopsins / Q000737:chemistry*; D016623:Ion Pumps / Q000737:chemistry*; D007700:Kinetics; D008027:Light; D010777:Photochemistry; D011487:Protein Conformation; D017494:Proton Pumps / Q000737:chemistry; D012545:Schiff Bases / Q000737:chemistry; D013055:Spectrophotometry, Infrared; D009626:Terminology as Topic
D016623:Ion Pumps; D017494:Proton Pumps; D012545:Schiff Bases; D001436:Bacteriorhodopsins