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PHOTOCHEMICAL ADDITION OF AMINO ACIDS AND PEPTIDES TO DNA
Author(s) -
SHETLAR MARTIN D.,
CHRISTENSEN JOHN,
HOM KELLIE
Publication year - 1984
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.1751-1097.1984.tb03417.x
Subject(s) - chemistry , amino acid , tryptophan , serine , phenylalanine , alanine , threonine , dna , aspartic acid , biochemistry , stereochemistry , phosphorylation
— The quantum yields for photochemical addition of twenty of the amino acids commonly occurring in proteins to denatured calf thymus DNA have been determined in deoxygenated phosphate buffer at λ 254 nM and pH 7 using a fluorescamine assay technique. Fifteen were found to be reactive, with cysteine, lysine, phenylalanine, tryptophan and tyrosine being the most reactive. Alanine, aspartic acid, glutamic acid, serine and threonine were unreactive. Analogous quantum yields for a series of eighteen peptides of the form glycyl X (X being one of the commonly occurring amino acids) were also determined, along with the corresponding quantum yields for L‐alanyl‐L‐alanine, L‐alanyl‐L‐tryptophan, L‐seryl‐L‐seryl‐L‐serine, L‐threonyl‐L‐threonyl‐L‐threonine, and L‐cystine‐ bis ‐glycine. All of the peptides were found to be reactive. The modified amino acids N ε ‐methyllysine, N ε , N ε , N ε ‐trimethyllysine and N ε ‐acetyllysine, all occurring in minor amounts in the histone group of chromosomal proteins, were also found to be reactive as was N α ‐acetyllysine. The quantum yields for photoaddition of a selected group of amino acids and peptides to denatured DNA and native DNA are compared. In some cases higher quantum yields for photoaddition to denatured DNA are observed while in other cases the reverse is true. The effect of oxygen on the quantum yields for photoaddition of selected peptides to DNA was examined. While for most systems studied the amount of reaction in aerated systems was less than in deoxygenated systems, in the case of glycyl‐L‐phenylalanine the reverse was true.