Methionine oxidation by hydrogen peroxide in peptides and proteins: A theoretical and Raman spectroscopy study

In this study the oxidation of the methionine residue using the tripeptide GlyMetGly with respect to hydrogen peroxide has been studied using both Raman spectroscopy and DFT calculations. Spectral modifications following the formation of methionine sulfoxide are shown with the appearance of the SO vibration whilst there is also the modification of the CS vibrations at approximately 700 cm−1. The changes in the intensity of the CS stretching band were used to calculate the kinetic rate constant as 7.9 ± 0.6 × 10−3 dm3 mol−1 s−1. The energy barrier for the reaction. is determined both experimentally and using DFT calculations. The reaction of the dairy protein beta-lactoglobulin with hydrogen peroxide is equally studied using the same technique. The solvent accessib...

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