Mesopone cytochrome c peroxidase: functional model of heme oxygenated oxidases

Direct Electrochemistry and Raman Spectroscopy of Sol−Gel-Encapsulated Myoglobin

“…The determination of the formal potentials of hemeproteins in physiologically relevant conditions is important since different physiological functions of proteins and redox behavior are usually related. − Controlling the oxidation state of the active-site metal (iron) of these proteins is fundamental to proper functioning as an oxygen-binding molecule. Measurements of peroxidase activities of many enzymes suggest that the enzymic activity correlates with the redox potential of the metal center. − A lower value of the Fe 3+ /Fe 2+ redox potential seems to be important for promoting peroxidase activity of the hemoprotein, possibly by stabilization of the high-valent redox intermediate involved in the catalytic function . In addition to that, it is important to carry out electrochemical studies of proteins to glean information concerning the thermodynamic and kinetic properties. − The field of fabricating biosensors and biomedical devices directly benefits from such measurements. , However, the determination of redox potentials of protein in the native form presents a major challenge due to the slow electron-transfer kinetics of the protein in a solution with a bare electrode .…”

“…Measurements of peroxidase activities of many enzymes suggest that the enzymic activity correlates with the redox potential of the metal center. [4][5][6] A lower value of the Fe 3+ /Fe 2+ redox potential seems to be important for promoting peroxidase activity of the hemoprotein, possibly by stabilization of the high-valent redox intermediate involved in the catalytic function. 7 In addition to that, it is important to carry out electrochemical studies of proteins to glean information concerning the thermodynamic and kinetic properties.…”

Composite films of lecithin and heme proteins with electrochemical and electrocatalytic activities

“…Controlling the oxidation state of the active-site metal (iron) of these proteins is fundamental to the probing of the function of oxygen-binding molecules. Measurements of the peroxidase activity of many proteins suggest that the enzymatic activity correlates with the redox potential of the metal center [4]. In light of this, it is important to carry out electrochemical studies of proteins to glean information concerning the thermodynamic and kinetic properties [5][6][7].…”