A proton pathway with large proton polarizability and the proton pumping mechanism in bacteriorhodopsin — Fourier transform difference spectra of photoproducts of bacteriorhodopsin and of its pentademethyl analogue
- 1 August 1992
- journal article
- Published by Elsevier in Journal of Molecular Structure
- Vol. 271 (3) , 157-173
- https://doi.org/10.1016/0022-2860(92)80123-y
Abstract
No abstract availableThis publication has 50 references indexed in Scilit:
- Bacteriorhodopsin in iceFEBS Letters, 1990
- Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffractionJournal of Molecular Biology, 1990
- Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopyJournal of Molecular Biology, 1990
- Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212Biochemistry, 1988
- Investigation of intramolecular processes in proteins by time resolved FTIR-difference spectroscopyMicrochimica Acta, 1988
- Only water‐exposed carboxyl groups are protonated during the transition to the cation‐free blue bacteriorhodopsinFEBS Letters, 1987
- Thermodynamics of proton transfer in carboxylic acid-retinal Schiff base hydrogen bonds with large proton polarizabilityBiochemical and Biophysical Research Communications, 1986
- Fourier-transform infrared difference spectroscopy of rhodopsin and its photoproducts at low temperatureBiochemistry, 1985
- Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation of static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membraneBiochemistry, 1985
- Light‐dependent reaction of bacteriorhodopsin with hydroxylamine in cell suspensions of Halobacterium halobium: Demonstration of an APO‐membraneFEBS Letters, 1974