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Sakmar, T. P., Franke, R. R., Khorana, H. G. (1991) The role of the retinylidene Schiff base counterion in rhodopsin in determining wavelength absorbance and Schiff base pKa. Proceedings of the National Academy of Sciences, 88 (8) 3079-3083 doi:10.1073/pnas.88.8.3079

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Reference TypeJournal (article/letter/editorial)
TitleThe role of the retinylidene Schiff base counterion in rhodopsin in determining wavelength absorbance and Schiff base pKa.
JournalProceedings of the National Academy of Sciences
AuthorsSakmar, T. P.Author
Franke, R. R.Author
Khorana, H. G.Author
Year1991 (April 15)Volume88
Issue8
PublisherProceedings of the National Academy of Sciences
DOIdoi:10.1073/pnas.88.8.3079Search in ResearchGate
Generate Citation Formats
Mindat Ref. ID1507249Long-form Identifiermindat:1:5:1507249:4
GUID0
Full ReferenceSakmar, T. P., Franke, R. R., Khorana, H. G. (1991) The role of the retinylidene Schiff base counterion in rhodopsin in determining wavelength absorbance and Schiff base pKa. Proceedings of the National Academy of Sciences, 88 (8) 3079-3083 doi:10.1073/pnas.88.8.3079
Plain TextSakmar, T. P., Franke, R. R., Khorana, H. G. (1991) The role of the retinylidene Schiff base counterion in rhodopsin in determining wavelength absorbance and Schiff base pKa. Proceedings of the National Academy of Sciences, 88 (8) 3079-3083 doi:10.1073/pnas.88.8.3079
In(1991, April) Proceedings of the National Academy of Sciences Vol. 88 (8) Proceedings of the National Academy of Sciences

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Sakmar, T. P., Franke, R. R., Khorana, H. G. (1989) Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proceedings of the National Academy of Sciences, 86 (21) 8309-8313 doi:10.1073/pnas.86.21.8309
Eilers, M., Reeves, P. J., Ying, W., Khorana, H. G., Smith, S. O. (1999) Magic angle spinning NMR of the protonated retinylidene Schiff base nitrogen in rhodopsin: Expression of 15N-lysine- and 13C-glycine-labeled opsin in a stable cell line. Proceedings of the National Academy of Sciences, 96 (2) 487-492 doi:10.1073/pnas.96.2.487
Longstaff, C., Calhoon, R. D., Rando, R. R. (1986) Deprotonation of the Schiff base of rhodopsin is obligate in the activation of the G protein. Proceedings of the National Academy of Sciences, 83 (12) 4209-4213 doi:10.1073/pnas.83.12.4209
Kusnetzow, A. K., Dukkipati, A., Babu, K. R., Ramos, L., Knox, B. E., Birge, R. R. (2004) Vertebrate ultraviolet visual pigments: Protonation of the retinylidene Schiff base and a counterion switch during photoactivation. Proceedings of the National Academy of Sciences, 101 (4) 941-946 doi:10.1073/pnas.0305206101
Doi, T., Molday, R. S., Khorana, H. G. (1990) Role of the intradiscal domain in rhodopsin assembly and function. Proceedings of the National Academy of Sciences, 87 (13) 4991-4995 doi:10.1073/pnas.87.13.4991
Otto, H., Marti, T., Holz, M., Mogi, T., Lindau, M., Khorana, H. G., Heyn, M. P. (1989) Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proceedings of the National Academy of Sciences, 86 (23) 9228-9232 doi:10.1073/pnas.86.23.9228
Dickopf, S., Alexiev, U., Krebs, M. P., Otto, H., Mollaaghababa, R., Khorana, H. G., Heyn, M. P. (1995) Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base state. Proceedings of the National Academy of Sciences, 92 (25) 11519-11523 doi:10.1073/pnas.92.25.11519
Karnik, S. S., Sakmar, T. P., Chen, H. B., Khorana, H. G. (1988) Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proceedings of the National Academy of Sciences, 85 (22) 8459-8463 doi:10.1073/pnas.85.22.8459
Otto, H., Marti, T., Holz, M., Mogi, T., Stern, L. J., Engel, F., Khorana, H. G., Heyn, M. P. (1990) Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff base. Proceedings of the National Academy of Sciences, 87 (3) 1018-1022 doi:10.1073/pnas.87.3.1018
Sineshchekov, O. A., Sasaki, J., Phillips, B. J., Spudich, J. L. (2008) A Schiff base connectivity switch in sensory rhodopsin signaling. Proceedings of the National Academy of Sciences, 105 (42) 16159-16164 doi:10.1073/pnas.0807486105
Thurmond, R. L., Creuzenet, C., Reeves, P. J., Khorana, H. G. (1997) Structure and function in rhodopsin: Peptide sequences in the cytoplasmic loops of rhodopsin are intimately involved in interaction with rhodopsin kinase. Proceedings of the National Academy of Sciences, 94 (5) 1715-1720 doi:10.1073/pnas.94.5.1715
 
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