The site of attachment of retinal in bacteriorhodopsin. The epsilon-amino group in Lys-41 is not required for proton translocation.

Content Provider	Semantic Scholar
Author	Huang, Kevin S. Liao, Mei-De Gupta, Chhitar M. Royal, Natalie Biemann, Klaus Khorana, Har Gobind
Copyright Year	1982
Abstract	Chymotryptic fragments C-1 (amino acids 72-248) and C-2 (amino acids 1-71) of bacteriorhodopsin have been shown previously to reassociate so as to regenerate the native bacteriorhodopsin chromophore in lipid/detergent mixtures and to form functional proton-translocating vesicles. The fragment C-2 has now been selectively methylated with formaldehyde and sodium cyanoborohydride to give the epsilon-dimethylamino derivatives of Lys-30, 40, and 41 in 96-99% average yield. The methylated and unmethylated C-2 fragments were identical in their ability to reassociate with fragment C-1 and retinal to regenerate the bacteriorhodopsin chromophore and to form functional proton-translocating vesicles. In contrast, dimethylation of the lysine residues of the C-1 fragment gave a derivative which did not form an active complex with unmethylated C-2. We conclude that the epsilon-amino group in Lys-41 is not required for Schiff's base formation with retinal at any step in the light-driven proton-translocation cycle.
File Format	PDF HTM / HTML
PubMed reference number	6284736
Journal	Medline
Volume Number	257
Issue Number	15
Alternate Webpage(s)	http://repository.ias.ac.in/15948/1/332.pdf
Journal	The Journal of biological chemistry
Language	English
Access Restriction	Open
Content Type	Text
Resource Type	Article