Protein Structure Influences Redox Stability, Oxygen Affinity, and Heat-Induced Denaturation Properties of Bovine Myoglobin, Hemoglobin, and Cytochrome <i>c</i>
Anuj Sharma, Runnan Li, Silan Bhandari, Surendranath P. Suman, Sadagopan Krishnan, Morgan Pfeiffer, G. G. Mafi, Ranjith Ramanathan
Abstract
High Resolution Image Download MS PowerPoint Slide While past research has predominantly focused on the role of myoglobin in meat color, investigations into the contributions of hemoglobin and cytochrome c are limited. Cytochrome c has the highest redox stability ( P < 0.05), followed by myoglobin and hemoglobin. Electrochemistry analysis revealed that cytochrome c has a greater capacity ( P < 0.05) to reduce than myoglobin and hemoglobin. Differential scanning calorimetry indicates that cytochrome c was most stable to heat ( P < 0.05), while no differences were noted between myoglobin and hemoglobin. Structural analysis noted that greater heat and redox stability of cytochrome c might be attributed to fewer histidine residues (3) and more covalent bonds (4) than myoglobin (13), hemoglobin α (10), and hemoglobin β (6). This study suggests that the amino acid sequence and number of covalent bonds can impact the redox stability and heat-induced denaturation properties of myoglobin, hemoglobin, and cytochrome c .