Abstract:
: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.
journal_name
Photochem Photobioljournal_title
Photochemistry and photobiologyauthors
Encinas MV,Lissi EA,Vasquez M,Olea AF,Silva Edoi
10.1111/j.1751-1097.1989.tb08424.xsubject
Has Abstractpub_date
1989-05-01 00:00:00pages
557-63issue
5eissn
0031-8655issn
1751-1097journal_volume
49pub_type
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