Ultraviolet-visible transient spectroscopy of bacteriorhodopsin mutants. Evidence for two forms of tyrosine-185—-phenylalanine.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference35 articles.
1. Effects of amino acid substitutions in the F helix of bacteriorhodopsin. Low temperature ultraviolet/visible difference spectroscopy.
2. Substitution of amino acids in helix F of bacteriorhodopsin: effects on the photochemical cycle
3. Resonance Raman evidence for an all-trans to 13-cis isomerization in the proton-pumping cycle of bacteriorhodopsin
4. Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
5. Vibrational spectroscopy of bacteriorhodopsin mutants: I. Tyrosine-185 protonates and deprotonantes during the photocycle
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1. Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2006-08
2. Time-Resolved Fourier Transform Infrared Spectroscopy of the Polarizable Proton Continua and the Proton Pump Mechanism of Bacteriorhodopsin;Biophysical Journal;2001-02
3. Nature of the Chromophore Binding Site of Bacteriorhodopsin: The Potential Role of Arg82 as a Principal Counterion;Biophysical Journal;1999-05
4. Biomolecular materials: structure, interactions and higher order self-assembly;Colloids and Surfaces A: Physicochemical and Engineering Aspects;1997-08
5. Threonine-89 Participates in the Active Site of Bacteriorhodopsin: Evidence for a Role in Color Regulation and Schiff Base Proton Transfer;Biochemistry;1997-06-01
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