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Abstract
Abstract— Results of a quantitative photochemical study of poly‐p‐benzoylphenylacetimido‐bovine serum albumin in the presence of small‐molecule triplet quenchers are reported. The efficiency of quenching by organic salts containing low triplet energy chromophores is shown to be qualitatively dependent on their predicted association constants to the modified protein. In addition, quenching is inhibited by salts of organic acids which possess high binding affinities for the protein but do not contain chromophores of low triplet energy. Quantitative treatment of the quenching and inhibition data yields results which strongly support the operation of an ‘affinity controlled’ mechanism for triplet energy transfer from the benzophenone moieties of the modified‐bovine serum albumin to quenchers such as α‐naphthylacetate and trans‐cinnamate.
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