Abstract
From pulse radiolysis measurements in oxygenated aqueous solution, the semioxidized tryptophan radical (Trp·— formed by the one-electron oxidation of Trp by Br 2 - radical—has been shown to oxidize the superoxide radical anion with a rate constant of k = 2 × 10 9 M −1 s −1. Proof of this reaction is found in addition of superoxide dismutase (SOD) to the system, which totally eliminates the contribution of the Trp · + O 2 - mechanism to Trp · decay. Little, if any, reaction of molecular oxygen with Trp · may be observed on the time scale of the pulse radiolysis experiment.
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