Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature.
- 1 January 1986
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 83 (2) , 347-351
- https://doi.org/10.1073/pnas.83.2.347
Abstract
Isotopically labeled tryosines have been selectively incorporated into bacteriorhodopsin (bR). A comparison of the low-temperature bR570 to K Fourier transform infrared-difference spectra of these samples and normal bR provides information about the role of tyrosine in the primary phototransition. Several tyrosine contributions to the difference spectrum are found. These results and comparison with the spectra of model compounds suggest that a tyrosinate group protonates during the bR570 to K transition. This conclusion is strongly supported by the results of UV difference spectroscopy.This publication has 28 references indexed in Scilit:
- Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopyPublished by Elsevier ,2005
- Hydrogen bonded chain mechanisms for proton conduction and proton pumpingThe Journal of Membrane Biology, 1983
- Investigation of the Primary Photochemistry of Bacteriorhodopsin by Low‐Temperature Fourier‐Transform Infrared SpectroscopyEuropean Journal of Biochemistry, 1983
- Fourier transform infrared difference spectroscopy of bacteriorhodopsin and its photoproducts.Proceedings of the National Academy of Sciences, 1982
- Infrared evidence that the Schiff base of bacteriorhodopsin is protonated: bR570 and K intermediates.Proceedings of the National Academy of Sciences, 1982
- Bacteriorhodopsin and Related Pigments of HalobacteriaAnnual Review of Biochemistry, 1982
- Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore.Proceedings of the National Academy of Sciences, 1982
- Proton conduction in bacteriophodopsin via a hydrogen-bonded chain with large proton polarizabilityBiochemical and Biophysical Research Communications, 1981
- Proton translocation in hydrogen bonds with large proton polarizability formed between a Schiff base and phenolsBiochemical and Biophysical Research Communications, 1981
- Resonance Raman spectroscopy of specifically [epsilon-15N]lysine-labeled bacteriorhodopsin.Proceedings of the National Academy of Sciences, 1981