Engineered manganese peroxidase model protein MP6.8 (MP6.8)

Engineered manganese peroxidase model protein MP6.8 is a synthetic enzyme variant designed to mimic the functional properties of native manganese peroxidases (MnP) found in white-rot fungi (Sundaramoorthy et al., 1998). It was constructed by modifying the protein scaffold of yeast cytochrome c peroxidase (CCP) to incorporate a manganese-binding site near the heme cofactor (Yeung et al., 1997). Key mutations, including G41D and V45D, were introduced to create a coordination environment where Mn(II) is ligated by an aspartate residue and a heme propionate (Sundaramoorthy et al., 1998). MP6.8 demonstrates the ability to catalyze the oxidation of Mn(II) to Mn(III) in the presence of hydrogen peroxide, following a catalytic cycle that involves high-valent ferryl heme intermediates (Sundaramoorthy et al., 1998). This model protein is primarily utilized in bioinorganic research to investigate the structural and electronic factors that govern manganese oxidation and to provide insights into the mechanisms of lignin biodegradation. It is not currently utilized as a therapeutic target or drug scaffold in clinical medicine, nor does it have a known role in human disease.

Other names

MP6.8CCP-MP6.8Manganese peroxidase model 6.8Cytochrome c peroxidase variant MP6.8

Not applicable as there are no drugs targeting this engineered model protein.