Deprotonation of tyrosines in bacteriorhodopsin as studied by Fourier transform infrared spectroscopy with deuterium and nitrate labeling
- 1 December 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 26 (25) , 8327-8331
- https://doi.org/10.1021/bi00399a045
Abstract
Note: In lieu of an abstract, this is the article's first page.Keywords
This publication has 18 references indexed in Scilit:
- Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts.Proceedings of the National Academy of Sciences, 1982
- ON THE ROLE OF TYROSINE IN THE PHOTOCYCLE OF BACTERIORHODOPSINPhotochemistry and Photobiology, 1982
- Reversible inhibition of the proton pump bacteriorhodopsin by modification of tyrosine 64.Journal of Biological Chemistry, 1982
- Infrared evidence that the Schiff base of bacteriorhodopsin is protonated: bR570 and K intermediates.Proceedings of the National Academy of Sciences, 1982
- The Role of Tyrosine Residues in the Function of BacteriorhodopsinEuropean Journal of Biochemistry, 1981
- Environmental effects on formation and photoreaction of the M412 photoproduct of bacteriorhodopsin: implications for the mechanism of proton pumpingBiochemistry, 1981
- Bacteriorhodopsin and the purple membrane of halobacteriaBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1979
- Isomeric Composition of Retinal Chromophore in Dark-Adapted Bacteriorhodopsin1The Journal of Biochemistry, 1977
- Resonance Raman studies of the purple membraneBiochemistry, 1977
- Identification of retinal isomers isolated from bacteriorhodopsinBiochemistry, 1977