Effect of iodination on the pK of Schiff base deprotonation and M412 production in purple membrane
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. Kinetic Resonance Raman Spectroscopy: Dynamics of Deprotonation of the Schiff Base of Bacteriorhodopsin
2. The pK of Schiff base deprotonation in bacteriorhodopsin
3. Resonance raman spectroscopy of chemically modified and isotopically labelled purple membranes. II. Kinetic studies
4. Photochemical cycle of bacteriorhodopsin studied by resonance Raman spectroscopy
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1. BIOSYNTHETIC INCORPORATION OF M-FLUOROTYROSINE INTO BACTERIORHODOPSIN;Photochemistry and Photobiology;1992-12
2. The mechanism of bacteriorhodopsin functioning. I. The light-induced proton throw-over by retinal;International Journal of Quantum Chemistry;1988-04
3. Bacteriorhodopsin mutants containing single tyrosine to phenylalanine substitutions are all active in proton translocation.;Proceedings of the National Academy of Sciences;1987-08-01
4. Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts regenerated with deuterated tyrosine;Biochemistry;1986-10
5. The chromophore-binding site of bacteriorhodopsin. Resonance Raman and surface-enhanced resonance Raman spectroscopy and quantum chemical study;Journal of Biosciences;1985-08
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