Protein-beta-ionone ring interactions enhance the light-induced dipole of the chromophore in bacteriorhodospin
Article Abstract:
The origin of protein effect by applying second harmonic generation measurements of artificial bacteriorhodopsin pigments derived from synthetic retinal analogues, characterized by a modified polyene chain length and ring-chain conformation is studied. The effect of tryptophane residues appear not only to stabilize the light-induced charge redistribution but also to enable the migration in the excited state of the positive charge into a region of the protein with a relatively low dielectric constant.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2003
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Photochemistry of a retinal protonated Schiff-base analogue mimicking the opsin shift of bacteriorhodopsin
Article Abstract:
Femtosecond multichannel pump probe spectroscopy is used to investigate a retinal Schiff base analogue that artificially mimics the protein-induced red shifting of absorption in bacteriorhodopsin (BR). The results have shown that the red shift afforded in the model system does not increase the internal conversion relative to free retinal-protonated Schiff base (RPSB) in solution.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2007
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Spin labeling of Natronomonas pharaonis halorhodopsin: Probing the cysteine residues environment
Article Abstract:
Halorhodopsin from Natronomonas pharaonis (pHR) is a light-driven chloride pump that transports a chloride anion across the plasma membrane following light absorption by a retinal chromophore, which initiates a photocycle. Analysis of the amino acid sequence of pHR reveals three cysteine residues (Cys160, Cys184, and Cys186) in helices D and E.
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
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