Meat color is associated with myoglobin content and redox state. Myoglobin is a water-soluble hemoprotein with iron in its prosthetic group, which determines myoglobin redox state by its valence state and ligand attached to the free coordination site. In fresh meat, myoglobin can be in three states in dynamic equilibrium: deoxymyoglobin, oxymyoglobin, and metmyoglobin. During meat product elaboration, myoglobin can chemically interact with several ingredients in the formulation, changing its redox state. These structural changes in myoglobin through processing conditions will affect its thermal stability and subsequently meat product color. Currently, cured meat products elaboration involves the use of sodium nitrite, a curing agent that reacts with myoglobin in meat, forming nitrosomyoglobin, which is a stable complex that confers a characteristic pink color to the final meat product. This work proposes a mathematical model that allows comprehension of myoglobin structural changes during an uncured meat product elaboration. Due to the phenomenological structure of the developed model, a valuable understanding is reached opening new alternatives to be considered in meat products' color, taking into account the myoglobin chemical state. The proposed phenomenological model is validated with an error of around 10%.