Formation of >C=O Bonds in the Radiation-induced Oxidation of Protein in Aqueous Systems

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Abstract

A SERIES of observations recently made indicate that formation of the >C=O bond is a principal chemical effect of the attack of hydroxyl radicals on protein in oxygenated solution. Irradiations were made in a neutron flux produced by bombardment of beryllium with 24-MeV. deuterons in the Crocker Laboratory 60-in. cyclotron. Solutions were exposed under one atmosphere of oxygen in sealed ‘Pyrex’ cells mounted in a motor-driven reel situated 15 cm. from the beryllium target. One of the cells in each exposure contained a formic acid–oxygen dosimeter1. (We employed the formic acid–oxygen dosimeter to obtain an estimate of the relative number of water molecules decomposed via (1) H2O = H + OH and (2) H2O = ½H2 + ½H2O2. Absolute yield values could then be calculated in terms of G(molecules/100 eV.), since in dilute solutions at pH values above 2.5, the sum G(1) + G(2) = G(H2O) is to a first approximation independent of the quality of the absorbed radiation1. With our standard geometry for neutron exposures, we obtained G(1) = 2.68, G(2) = 0.97 on the basis of G(H2O) = 3.652.)

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JAYKO, M., GARRISON, W. Formation of >C=O Bonds in the Radiation-induced Oxidation of Protein in Aqueous Systems. Nature 181, 413–414 (1958) doi:10.1038/181413a0

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