Ultraviolet resonance Raman spectroscopy of bacteriorhodopsin: evidence against tyrosinate in the photocycle

Ultraviolet resonance Raman (UVRR) spectroscopy is a powerful technique for probing the structure of proteins. Vibrational scattering from different aromatic residues may be selectively enhanced by choosing appropriate excitation wavelengths. This raises the attractive possibility of using UVRR to s...

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Bibliographic Details
Published in:Journal of the American Chemical Society 1990-11, Vol.112 (24), p.9007-9009
Main Authors: Ames, James B, Bolton, Sarah R, Netto, Madeline M, Mathies, Richard A
Format: Article
Language:English
Subjects:
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Molecular biophysics
Photochemistry. Photosynthesis. Bioluminescence
protons
Radiation-biomolecule interaction
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Summary:Ultraviolet resonance Raman (UVRR) spectroscopy is a powerful technique for probing the structure of proteins. Vibrational scattering from different aromatic residues may be selectively enhanced by choosing appropriate excitation wavelengths. This raises the attractive possibility of using UVRR to study dynamic structural changes in proteins such as bacteriorhodopsin (BR), which functions as a light-driven proton pump. It was previously proposed that light-adapted bacteriorhodopsin (BR sub(568)) contains an ionized tyrosine (Tyr-185) which protonates upon light absorption and when the protein relaxes to its dark-adapted state (BR sub(DA)). We present UVRR spectra of BR sub(568) and BR sub(DA) which indicate that tyrosinate does not play a role in the photocycle.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja00180a071