PHOTOINTERACTION OF BENZOPHENONE TRIPLET WITH LYSOZYME

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dc.contributor.authorENCINAS, MV
dc.contributor.authorLISSI, EA
dc.contributor.authorVASQUEZ, M
dc.contributor.authorOLEA, AF
dc.contributor.authorSILVA, E
dc.date.accessioned2025-01-23T19:24:00Z
dc.date.available2025-01-23T19:24:00Z
dc.date.issued1989
dc.description.abstractThe 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 .times. 109 M-1s-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 .times. 109 M-1s-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 tryosine and methionine groups are also consumed.
dc.fuente.origenWOS
dc.identifier.eissn1751-1097
dc.identifier.issn0031-8655
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99294
dc.identifier.wosidWOS:A1989U532100005
dc.issue.numero5
dc.language.isoen
dc.pagina.final563
dc.pagina.inicio557
dc.revistaPhotochemistry and photobiology
dc.rightsacceso restringido
dc.titlePHOTOINTERACTION OF BENZOPHENONE TRIPLET WITH LYSOZYME
dc.typeartículo
dc.volumen49
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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