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Analysis of photooxidized pigments in water-soluble chlorophyll protein complex isolated from Chenopodium album

Paper ID Volume ID Publish Year Pages File Format Full-Text
28446 44075 2006 5 PDF Available
Title
Analysis of photooxidized pigments in water-soluble chlorophyll protein complex isolated from Chenopodium album
Abstract

A water-soluble chlorophyll (Chl) protein complex isolated from Chenopodium album is converted to another form of the pigment protein (CP740) containing bacteriochlorin type pigments by irradiation with visible light in an aqueous aerated solution. In order to investigate the photoconverted pigments in CP740, all the chlorophyllous pigments were extracted with organic solvents from CP740 and were analyzed by high-performance liquid chromatography and mass spectrometry. Two separated products were mono-oxygen adducts to Chl a at the B-ring. Their visible spectral analysis combined with model calculation supported that they would be 8-oxo- (P700) and 7,8-epoxy-derivatives (P726). During extraction, covalent bonds of pigments with proteins in CP740 would be cleaved to produce the above mono-oxygenated Chls a. Based on the molecular structures of P700 and P726, bacteriochlorophyll type pigments in CP740 were proposed.

Keywords
Bacteriochlorin; Chlorophyll; Photooxidation; Photoreaction; Photosensitization
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Analysis of photooxidized pigments in water-soluble chlorophyll protein complex isolated from Chenopodium album
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology A: Chemistry - Volume 183, Issues 1–2, 30 September 2006, Pages 121–125
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
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Price was $35.95
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