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. 1993 Feb 15;90(4):1166–1171. doi: 10.1073/pnas.90.4.1166

Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin.

H G Khorana 1
PMCID: PMC45834  PMID: 8433978

Abstract

Site-directed mutagenesis has provided insight into the mechanisms of action of bacteriorhodopsin and rhodopsin. These studies are summarized here.

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Selected References

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

  1. Bennett N., Michel-Villaz M., Kühn H. Light-induced interaction between rhodopsin and the GTP-binding protein. Metarhodopsin II is the major photoproduct involved. Eur J Biochem. 1982 Sep;127(1):97–103. doi: 10.1111/j.1432-1033.1982.tb06842.x. [DOI] [PubMed] [Google Scholar]
  2. Braiman M. S., Mogi T., Marti T., Stern L. J., Khorana H. G., Rothschild K. J. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212. Biochemistry. 1988 Nov 15;27(23):8516–8520. doi: 10.1021/bi00423a002. [DOI] [PubMed] [Google Scholar]
  3. Butt H. J., Fendler K., Bamberg E., Tittor J., Oesterhelt D. Aspartic acids 96 and 85 play a central role in the function of bacteriorhodopsin as a proton pump. EMBO J. 1989 Jun;8(6):1657–1663. doi: 10.1002/j.1460-2075.1989.tb03556.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Doi T., Molday R. S., Khorana H. G. Role of the intradiscal domain in rhodopsin assembly and function. Proc Natl Acad Sci U S A. 1990 Jul;87(13):4991–4995. doi: 10.1073/pnas.87.13.4991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ferretti L., Karnik S. S., Khorana H. G., Nassal M., Oprian D. D. Total synthesis of a gene for bovine rhodopsin. Proc Natl Acad Sci U S A. 1986 Feb;83(3):599–603. doi: 10.1073/pnas.83.3.599. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Franke R. R., Sakmar T. P., Graham R. M., Khorana H. G. Structure and function in rhodopsin. Studies of the interaction between the rhodopsin cytoplasmic domain and transducin. J Biol Chem. 1992 Jul 25;267(21):14767–14774. [PubMed] [Google Scholar]
  7. Greenhalgh D. A., Subramaniam S., Alexiev U., Otto H., Heyn M. P., Khorana H. G. Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsin. J Biol Chem. 1992 Dec 25;267(36):25734–25738. [PubMed] [Google Scholar]
  8. Hackett N. R., Stern L. J., Chao B. H., Kronis K. A., Khorana H. G. Structure-function studies on bacteriorhodopsin. V. Effects of amino acid substitutions in the putative helix F. J Biol Chem. 1987 Jul 5;262(19):9277–9284. [PubMed] [Google Scholar]
  9. Henderson R., Baldwin J. M., Ceska T. A., Zemlin F., Beckmann E., Downing K. H. Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy. J Mol Biol. 1990 Jun 20;213(4):899–929. doi: 10.1016/S0022-2836(05)80271-2. [DOI] [PubMed] [Google Scholar]
  10. Henderson R., Unwin P. N. Three-dimensional model of purple membrane obtained by electron microscopy. Nature. 1975 Sep 4;257(5521):28–32. doi: 10.1038/257028a0. [DOI] [PubMed] [Google Scholar]
  11. Holz M., Drachev L. A., Mogi T., Otto H., Kaulen A. D., Heyn M. P., Skulachev V. P., Khorana H. G. Replacement of aspartic acid-96 by asparagine in bacteriorhodopsin slows both the decay of the M intermediate and the associated proton movement. Proc Natl Acad Sci U S A. 1989 Apr;86(7):2167–2171. doi: 10.1073/pnas.86.7.2167. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Karnik S. S., Khorana H. G. Assembly of functional rhodopsin requires a disulfide bond between cysteine residues 110 and 187. J Biol Chem. 1990 Oct 15;265(29):17520–17524. [PubMed] [Google Scholar]
  13. Karnik S. S., Sakmar T. P., Chen H. B., Khorana H. G. Cysteine residues 110 and 187 are essential for the formation of correct structure in bovine rhodopsin. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8459–8463. doi: 10.1073/pnas.85.22.8459. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Khorana H. G. Bacteriorhodopsin, a membrane protein that uses light to translocate protons. J Biol Chem. 1988 Jun 5;263(16):7439–7442. [PubMed] [Google Scholar]
  15. König B., Arendt A., McDowell J. H., Kahlert M., Hargrave P. A., Hofmann K. P. Three cytoplasmic loops of rhodopsin interact with transducin. Proc Natl Acad Sci U S A. 1989 Sep;86(18):6878–6882. doi: 10.1073/pnas.86.18.6878. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Mathies R. A., Lin S. W., Ames J. B., Pollard W. T. From femtoseconds to biology: mechanism of bacteriorhodopsin's light-driven proton pump. Annu Rev Biophys Biophys Chem. 1991;20:491–518. doi: 10.1146/annurev.bb.20.060191.002423. [DOI] [PubMed] [Google Scholar]
  17. Mogi T., Marti T., Khorana H. G. Structure-function studies on bacteriorhodopsin. IX. Substitutions of tryptophan residues affect protein-retinal interactions in bacteriorhodopsin. J Biol Chem. 1989 Aug 25;264(24):14197–14201. [PubMed] [Google Scholar]
  18. Mogi T., Stern L. J., Chao B. H., Khorana H. G. Structure-function studies on bacteriorhodopsin. VIII. Substitutions of the membrane-embedded prolines 50, 91, and 186: the effects are determined by the substituting amino acids. J Biol Chem. 1989 Aug 25;264(24):14192–14196. [PubMed] [Google Scholar]
  19. Mogi T., Stern L. J., Hackett N. R., Khorana H. G. Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5595–5599. doi: 10.1073/pnas.84.16.5595. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Mogi T., Stern L. J., Marti T., Chao B. H., Khorana H. G. Aspartic acid substitutions affect proton translocation by bacteriorhodopsin. Proc Natl Acad Sci U S A. 1988 Jun;85(12):4148–4152. doi: 10.1073/pnas.85.12.4148. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Nagle J. F., Morowitz H. J. Molecular mechanisms for proton transport in membranes. Proc Natl Acad Sci U S A. 1978 Jan;75(1):298–302. doi: 10.1073/pnas.75.1.298. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Nathans J., Davenport C. M., Maumenee I. H., Lewis R. A., Hejtmancik J. F., Litt M., Lovrien E., Weleber R., Bachynski B., Zwas F. Molecular genetics of human blue cone monochromacy. Science. 1989 Aug 25;245(4920):831–838. doi: 10.1126/science.2788922. [DOI] [PubMed] [Google Scholar]
  23. Nathans J. Determinants of visual pigment absorbance: identification of the retinylidene Schiff's base counterion in bovine rhodopsin. Biochemistry. 1990 Oct 16;29(41):9746–9752. doi: 10.1021/bi00493a034. [DOI] [PubMed] [Google Scholar]
  24. Oesterhelt D., Tittor J. Two pumps, one principle: light-driven ion transport in halobacteria. Trends Biochem Sci. 1989 Feb;14(2):57–61. doi: 10.1016/0968-0004(89)90044-3. [DOI] [PubMed] [Google Scholar]
  25. Oprian D. D., Molday R. S., Kaufman R. J., Khorana H. G. Expression of a synthetic bovine rhodopsin gene in monkey kidney cells. Proc Natl Acad Sci U S A. 1987 Dec;84(24):8874–8878. doi: 10.1073/pnas.84.24.8874. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Otto H., Marti T., Holz M., Mogi T., Lindau M., Khorana H. G., Heyn M. P. Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9228–9232. doi: 10.1073/pnas.86.23.9228. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Otto H., Marti T., Holz M., Mogi T., Stern L. J., Engel F., Khorana H. G., Heyn M. P. 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. Proc Natl Acad Sci U S A. 1990 Feb;87(3):1018–1022. doi: 10.1073/pnas.87.3.1018. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Sakmar T. P., Franke R. R., Khorana H. G. Glutamic acid-113 serves as the retinylidene Schiff base counterion in bovine rhodopsin. Proc Natl Acad Sci U S A. 1989 Nov;86(21):8309–8313. doi: 10.1073/pnas.86.21.8309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Stern L. J., Khorana H. G. Structure-function studies on bacteriorhodopsin. X. Individual substitutions of arginine residues by glutamine affect chromophore formation, photocycle, and proton translocation. J Biol Chem. 1989 Aug 25;264(24):14202–14208. [PubMed] [Google Scholar]
  30. Stoeckenius W., Bogomolni R. A. Bacteriorhodopsin and related pigments of halobacteria. Annu Rev Biochem. 1982;51:587–616. doi: 10.1146/annurev.bi.51.070182.003103. [DOI] [PubMed] [Google Scholar]
  31. Stoeckenius W., Lozier R. H., Bogomolni R. A. Bacteriorhodopsin and the purple membrane of halobacteria. Biochim Biophys Acta. 1979 Mar 14;505(3-4):215–278. doi: 10.1016/0304-4173(79)90006-5. [DOI] [PubMed] [Google Scholar]
  32. Subramaniam S., Greenhalgh D. A., Khorana H. G. Aspartic acid 85 in bacteriorhodopsin functions both as proton acceptor and negative counterion to the Schiff base. J Biol Chem. 1992 Dec 25;267(36):25730–25733. [PubMed] [Google Scholar]
  33. Subramaniam S., Marti T., Rösselet S. J., Rothschild K. J., Khorana H. G. The reaction of hydroxylamine with bacteriorhodopsin studied with mutants that have altered photocycles: selective reactivity of different photointermediates. Proc Natl Acad Sci U S A. 1991 Mar 15;88(6):2583–2587. doi: 10.1073/pnas.88.6.2583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Wald G. The molecular basis of visual excitation. Nature. 1968 Aug 24;219(5156):800–807. doi: 10.1038/219800a0. [DOI] [PubMed] [Google Scholar]
  35. Wilden U., Hall S. W., Kühn H. Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments. Proc Natl Acad Sci U S A. 1986 Mar;83(5):1174–1178. doi: 10.1073/pnas.83.5.1174. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Zhukovsky E. A., Oprian D. D. Effect of carboxylic acid side chains on the absorption maximum of visual pigments. Science. 1989 Nov 17;246(4932):928–930. doi: 10.1126/science.2573154. [DOI] [PubMed] [Google Scholar]

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