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REACTIVITY OF SINGLET OXYGEN TOWARD AMINO ACIDS AND PEPTIDES
Author(s) -
Michaeli Albert,
Feitelson Jehuda
Publication year - 1994
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.1751-1097.1994.tb05035.x
Subject(s) - singlet oxygen , reactivity (psychology) , chemistry , amino acid , oxygen , singlet state , photochemistry , biochemistry , organic chemistry , physics , medicine , nuclear physics , alternative medicine , pathology , excited state
Quenching of singlet oxygen ( 1 O 2 ) in D 2 O‐ethanol by the amino acids tryptophan, tyrosine, histidine, methionine, cysteine and their derivatives was measured by exciting the sensitizers rose bengal or meso ‐tetra ( N ‐methyl‐4‐pyridyl)porphyrin tetratosylate in the presence of oxygen and the above quenchers in solution. In our polar solvent, containing 75% D 2 O on a molar basis it was found that (1) substitution of the aromatic ring in indole, phenol and imidazole by the electron‐donating methyl group increases the total ( i.e. nonreactive and reactive) quenching rate constant by a factor of five to eight. Free or blocked amino and carboxyl groups removed by two methylene groups from the ring counteract the above increase in the rate constant. The reactive quenching of singlet oxygen, which leads to oxidative destruction of the aromatic ring, correlates with the above substitution effects. It has been proposed that the quenching process takes place by formation of an exciplex between 1 O 2 and the quencher. Thus our results indicate that the better an electron donor the amino acid residue is the more pronounced is the charge transfer contribution in the exciplex formed with 1 O 2 and the more likely it is to lead to charge separation and hence to a chemical reaction. (2) Oligopeptides in solution or peptide bonds linked to the amino acid residue have only a minor effect on singlet oxygen. It can therefore be expected that the polypeptide chains per se in the protein network will not interact significantly with the single oxygen molecules present. The quenching of the latter should, to a first approximation, depend only on the presence of the above reactive amino acid residues and to their accessibility to 1 O 2 as well as on the effective dielectric constant within the protein structure.