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. 1988 Sep;54(3):557–562. doi: 10.1016/S0006-3495(88)82989-8

Photochemistry of monomethylated and permethylated bacteriorhodopsin.

R Govindjee 1, Z Dancshazy 1, T G Ebrey 1, C Longstaff 1, R R Rando 1
PMCID: PMC1330355  PMID: 3207841

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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