Photochemistry of monomethylated and permethylated bacteriorhodopsin.
Methylation of the nonactive site lysines of bacteriorhodopsin to form permethylated bacteriorhodopsin does not interfere with the formation of the short wavelength intermediate M412 or light-induced proton release/uptake. The absorption spectrum is similar to that of the native bacteriorhodopsin. However, additional monomethylation of the active site lysine of bacteriorhodopsin causes a red shift of the absorption maximum from 568 nm in light-adapted bacteriorhodopsin [BR] to 630 nm. The photochemistry of active-site methylated BR does not proceed beyond the L-photointermediate. In particular, the photointermediate corresponding to M412 does not form, and there is no proton pumping. Moreover, there is no tyrosine deprotonation. Thus, the formation of an M-type photointermediate is required for proton pumping by BR.
Govindjee
R
R
Department of Physiology, University of Illinois, Urbana 61801.
Dancshazy
Z
Z
Ebrey
T G
TG
Longstaff
C
C
Rando
R R
RR
D001436:Bacteriorhodopsins / Q000031:analogs & derivatives* / Q000378:metabolism* / Q000528:radiation effects; D006217:Halobacterium / Q000378:metabolism; D007700:Kinetics; D007834:Lasers; D008745:Methylation; D010777:Photochemistry; D013053:Spectrophotometry
D001436:Bacteriorhodopsins