The hydroxyl radical oxidation system (0.01 mmol/L FeCl3， 0.1 mmol/L ascorbic acid， H2O₂) was employed in this study to investigate the effects of H2O₂ concentration (0， 10， 30， 50， 70 mmol/L) on the oxidation and nitrosation of pork myofibrillar protein (MP). Results showed that with the increase of H2O₂ concentration， the protein carbonyl content， disulfide bond level， dityrosine， 3-nitrotyrosine (3-NT)， N-nitrosodiethylamine (NDEA) and N-nitrosodimethylamine (NDMA) content were increased， while the contents of total sulfhydryl groups， free amino groups and the residual amount of NaNO₂ were decreased. The relationship between indexes of protein oxidation and nitrosation was assessed by pearson correlation coefficient. N-nitrosamine and 3-NT content within MP significantly positively correlated with carbonyl， disulfide bond and dityrosine content (P<0.05)， but negatively correlated with total sulfhydryl groups and free amino groups (P<0.05). These results indicated that 3-NT may be a potential marker of protein oxidation and nitrosation. Our results demonstrated that protein oxidation could promote protein nitrosation and consequent NDMA and NDEA formation. Therefore， protein oxidation and nitrosation should be controlled during meat processing and storage to control the formation of N-nitrosamine.