Alteration of pKa of the bacteriorhodopsin protonated Schiff base. A study with model compounds
- 1 September 1986
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 25 (18) , 5249-5258
- https://doi.org/10.1021/bi00366a040
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Bacteriorhodopsins with chromophores modified at the β‐ionone siteEuropean Journal of Biochemistry, 1984
- Acid-base equilibrium of the Schiff base in bacteriorhodopsinBiochemistry, 1982
- Energy storage and reaction pathways in the first step of the vision processJournal of the American Chemical Society, 1982
- Theoretical calculations on proton-transfer energetics: studies of methanol, imidazole, formic acid, and methaneethiol as models for the serine and cysteine proteasesJournal of the American Chemical Society, 1981
- Proton translocation in hydrogen bonds with large proton polarizability formed between a Schiff base and phenolsBiochemical and Biophysical Research Communications, 1981
- Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumpingBiochemistry, 1981
- THE INVOLVEMENT OF WATER AT THE RETINAL BINDING SITE IN RHODOPSIN AND EARLY LIGHT-INDUCED INTRAMOLECULAR PROTON TRANSFERPhotochemistry and Photobiology, 1981
- Photoisomerization, energy storage, and charge separation: A model for light energy transduction in visual pigments and bacteriorhodopsinProceedings of the National Academy of Sciences, 1979
- Bacteriorhodopsin and the purple membrane of halobacteriaBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1979
- Specificity of the retinal binding site of bacteriorhodopsin: chemical and stereochemical requirements for the binding of retinol and retinalBiochemistry, 1978