Resonance Raman studies on the intermediate K-590 in the photocycle of bacteriorhodopsin

Resonance Raman (RR) spectra of the intermediate K-590 in the photocycle of the retinylidene Schiff base chromophore of bacteriorhodopsin (BR) were recorded at 21{degree}C, where K has a lifetime of {approximately}2 {mu}s. An aqueous suspension of purple membranes from Halobacteria (16 {mu}M concent...

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Veröffentlicht in:Journal of physical chemistry (1952) 1991-03, Vol.95 (5), p.1993-2001
Hauptverfasser: Lohrmann, R, Grieger, I, Stockburger, Manfred
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container_end_page 2001
container_issue 5
container_start_page 1993
container_title Journal of physical chemistry (1952)
container_volume 95
creator Lohrmann, R
Grieger, I
Stockburger, Manfred
description Resonance Raman (RR) spectra of the intermediate K-590 in the photocycle of the retinylidene Schiff base chromophore of bacteriorhodopsin (BR) were recorded at 21{degree}C, where K has a lifetime of {approximately}2 {mu}s. An aqueous suspension of purple membranes from Halobacteria (16 {mu}M concentration of BR) was flowed across the waist of a laser beam (514 nm) serving for both photolysis and RR excitation. The residence time of the sample in the beam waist was {approximately}2 {mu}s. To subtract the contribution of the parent BR-570, a special experiment was designed in which two spectra, one at a low degree of photolysis (mainly consisting of BR-570) and one at a significantly higher degree of photolysis (mixture of BR-570 and K-590) could be recorded simultaneously. This allowed us to perform the difference procedure with high accuracy. New vibrational features in the spectrum of K-590 were identified in the C{double bond}C stretching region. From a comparison with the RR spectra of the parent BR-570 and the subsequent product L-550 the following was concluded: During the photoinduced transition from BR-570 to K-590 a negatively charged counterion is removed from the positively charged Schiff base group.
doi_str_mv 10.1021/j100158a020
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An aqueous suspension of purple membranes from Halobacteria (16 {mu}M concentration of BR) was flowed across the waist of a laser beam (514 nm) serving for both photolysis and RR excitation. The residence time of the sample in the beam waist was {approximately}2 {mu}s. To subtract the contribution of the parent BR-570, a special experiment was designed in which two spectra, one at a low degree of photolysis (mainly consisting of BR-570) and one at a significantly higher degree of photolysis (mixture of BR-570 and K-590) could be recorded simultaneously. This allowed us to perform the difference procedure with high accuracy. New vibrational features in the spectrum of K-590 were identified in the C{double bond}C stretching region. 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Phys. Chem</addtitle><description>Resonance Raman (RR) spectra of the intermediate K-590 in the photocycle of the retinylidene Schiff base chromophore of bacteriorhodopsin (BR) were recorded at 21{degree}C, where K has a lifetime of {approximately}2 {mu}s. An aqueous suspension of purple membranes from Halobacteria (16 {mu}M concentration of BR) was flowed across the waist of a laser beam (514 nm) serving for both photolysis and RR excitation. The residence time of the sample in the beam waist was {approximately}2 {mu}s. To subtract the contribution of the parent BR-570, a special experiment was designed in which two spectra, one at a low degree of photolysis (mainly consisting of BR-570) and one at a significantly higher degree of photolysis (mixture of BR-570 and K-590) could be recorded simultaneously. This allowed us to perform the difference procedure with high accuracy. New vibrational features in the spectrum of K-590 were identified in the C{double bond}C stretching region. 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Phys. Chem</addtitle><date>1991-03</date><risdate>1991</risdate><volume>95</volume><issue>5</issue><spage>1993</spage><epage>2001</epage><pages>1993-2001</pages><issn>0022-3654</issn><eissn>1541-5740</eissn><coden>JPCHAX</coden><abstract>Resonance Raman (RR) spectra of the intermediate K-590 in the photocycle of the retinylidene Schiff base chromophore of bacteriorhodopsin (BR) were recorded at 21{degree}C, where K has a lifetime of {approximately}2 {mu}s. An aqueous suspension of purple membranes from Halobacteria (16 {mu}M concentration of BR) was flowed across the waist of a laser beam (514 nm) serving for both photolysis and RR excitation. The residence time of the sample in the beam waist was {approximately}2 {mu}s. To subtract the contribution of the parent BR-570, a special experiment was designed in which two spectra, one at a low degree of photolysis (mainly consisting of BR-570) and one at a significantly higher degree of photolysis (mixture of BR-570 and K-590) could be recorded simultaneously. This allowed us to perform the difference procedure with high accuracy. New vibrational features in the spectrum of K-590 were identified in the C{double bond}C stretching region. From a comparison with the RR spectra of the parent BR-570 and the subsequent product L-550 the following was concluded: During the photoinduced transition from BR-570 to K-590 a negatively charged counterion is removed from the positively charged Schiff base group.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><doi>10.1021/j100158a020</doi><tpages>9</tpages></addata></record>
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source ACS Publications
subjects 140505 - Solar Energy Conversion- Photochemical, Photobiological, & Thermochemical Conversion- (1980-)
400500 - Photochemistry
Analytical, structural and metabolic biochemistry
Biological and medical sciences
CHEMICAL REACTIONS
DATA
DATA ANALYSIS
EXPERIMENTAL DATA
Fundamental and applied biological sciences. Psychology
INFORMATION
INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY
LASER SPECTROSCOPY
MEASURING METHODS
MEDIUM TEMPERATURE
NUMERICAL DATA
PHOTOCHEMICAL REACTIONS
PHOTOSYNTHESIS
PHOTOSYNTHETIC BACTERIA
Proteins
RAMAN SPECTROSCOPY
SOLAR ENERGY
SPECTROSCOPY
SYNTHESIS
title Resonance Raman studies on the intermediate K-590 in the photocycle of bacteriorhodopsin
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