THE QUENCHING OF SINGLET OXYGEN BY AMINO ACIDS AND PROTEINS

Abstract

Abstract— The physical quenching of singlet molecular oxygen (1 Δ g) by amino acids and proteins in D 2 O solution has been measured by their inhibition of the rate of singlet oxygen oxidation of the bilirubin anion. Steady‐state singlet oxygen concentrations are produced by irradiating the oxygenated solution with the 1–06 μm output of a Nd‐YAG laser, which absorbs directly in the electronic transition 1 Δ g+ 1 v→3 Σ g‐. The rate of quenching by most of the proteins studied is approximated by the sum of the quenching rates of their amino acids histidine, tryptophan and methionine, which implies that these amino acids in the protein structure are all about equally accessible to the singlet oxygen. The quenching constants differ from those obtained by the ruby‐laser methylene‐blue‐photosensitized method of generating singlet oxygen, or from the results of steady‐state methylene‐blue‐photosensitized oxidation, where singlet oxygen is assumed to be the main reactive species. The singlet oxygen quenching rates in D 2 O, pD 8, are (10 7? mol‐1 s‐1): alanine 0–2, methionine 3, tryptophan 9, histidine 17, carbonic anhydrase 85, lysozyme 150, superoxide dismutase 260, aposuperoxide dismutase 250.