Photointeraction of benzophenone triplet with lysozyme.
The quenching of the benzophenone triplet by lysozyme and its constituent amino acids in aqueous solutions have been studied. Native lysozyme quenches the benzophenone triplet with a high rate constant, 4 x 10(9) M-1 s-1. The quenching process takes place with production of significant amounts of free ketyl radicals, phi ketyl = 0.56, but with a very low benzophenone consumption yield (0.022). The consumption yield is considerably smaller than that observed for the free amino acids. This difference can be explained in terms of a dominant back hydrogen transfer to the protein in the disproportionation of the free radicals produced. Reduced and carboxymethylated lysozyme shows a higher quenching rate (7.8 x 10(9) M-1 s-1) and a larger benzophenone consumption yield (0.07). The deactivation of the benzophenone triplet by the native protein leads to its inactivation, with a quantum yield of 0.01. Tryptophan and arginine residues are destroyed with a quantum yield of 0.01. In the modified enzyme tyrosine and methionine groups are also consumed.
Encinas
M V
MV
Lissi
E A
EA
Vasquez
M
M
Olea
A F
AF
Silva
E
E
D000596:Amino Acids; D001577:Benzophenones; D009113:Muramidase; D010777:Photochemistry; D013057:Spectrum Analysis
D000596:Amino Acids; D001577:Benzophenones; D009113:Muramidase