(1) To electrochemically determine the species-dependent (beef, pork, and chicken) metmyoglobin reduction (relates to discoloration of meat) and oxygenation (relates to bloom or red color formation) properties with respect to different oxygen levels, pH conditions, and temperature. Once the animal is harvested, depending on the antioxidant levels left, the metmyoglobin concentration is decided due to the undesired conversion from oxymyoglobin upon diminishing antioxidants activity. Therefore, the proposed approach of measuring the reduction potential parameter will quantitatively infer the composition of metmyoglobin and oxymyoglobin in meat as a highly reliable new intrinsic molecular approach. Using the characteristics peak potentials that is from NADH or electrode, we will study the effect of adding NADH to the system to quantitatively measure the extent of currents at the NADH peak potential.(2) To validate the outcome of electrochemical redox kinetics of myoglobin from different species with standard spectrophotometric assays and the meat model system. We will compare the turnover rates from the electrochemical and spectroscopic methods, which helps normalizing the differences in the methodologies used (the PD's prior related paper for this comparison procedure for electrochemical vs. NADPH cytochrome P450 assay is given here to support feasibility of the comparison: J. Am. Chem. Soc. 2011, 133, 1459-1465).