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Flavin‐sensitized Photo‐oxidation of Lysozyme and Serum Albumin
Author(s) -
Zhang Yazhou,
Görner Helmut
Publication year - 2009
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.2009.00547.x
Subject(s) - flavin group , chemistry , photochemistry , flavin mononucleotide , lysozyme , quenching (fluorescence) , riboflavin , triplet state , electron transfer , bovine serum albumin , flavoprotein , moiety , singlet oxygen , tryptophan , flavin adenine dinucleotide , oxygen , fluorescence , cofactor , stereochemistry , organic chemistry , biochemistry , molecule , enzyme , physics , amino acid , quantum mechanics
The excited state processes of riboflavin, flavin mononucleotide and flavin adenine dinucleotide in argon‐saturated aqueous solution were studied in the presence of lysozyme or bovine serum albumin (BSA). UV–Vis absorption and fluorescence spectroscopy indicates that the noncovalent flavin‐protein binding is relatively weak. Quenching of the flavin triplet state by BSA, observed by time‐resolved photolysis, is less efficient than by lysozyme. Light‐induced oxidation of the two proteins and reduction of the three flavins were studied. The quantum yields of the former and latter in the absence of oxygen are up to 0.1 and 0.04, respectively. The effects of pH and sensitizer and protein concentrations were examined in greater detail. The proposed reaction is electron transfer from the tryptophan moiety to the flavin triplet rather than excited singlet state.