title: Redox active molecules cytochrome c and vitamin C enhance heme-enzyme peroxidations by serving as non-specific agents for redox relay.
abstract: We report that incorporation of very low concentrations of redox protein cytochrome c and redox active small molecule vitamin C impacted the outcome of one-electron oxidations mediated by structurally distinct plant/fungal heme peroxidases. Evidence suggests that cytochrome c and vitamin C function as a redox relay for diffusible reduced oxygen species in the reaction system, without invoking specific or affinity-based molecular interactions for electron transfers. The findings provide novel perspectives to understanding - (1) the promiscuous role of cytochrome b(5) in the metabolism mediated by liver microsomal xenobiotic metabolizing systems and (2) the roles of antioxidant molecules in affording relief from oxidative stress.
authors.affiliation: Heme & Flavo Proteins Laboratory, #204, Center for Biomedical Research, VIT University, Vellore, Tamil Nadu 632014, India.
authors.forename: Sudeep Kumar
authors.initials: SK
authors.lastname: Gade
authors.forename: Subarna
authors.initials: S
authors.lastname: Bhattacharya
authors.forename: Kelath Murali
authors.initials: KM
authors.lastname: Manoj
mesh_terms: D000975:Antioxidants / Q000737:chemistry*; D001205:Ascorbic Acid / Q000737:chemistry*; D002711:Chloride Peroxidase / Q000737:chemistry*; D045304:Cytochromes c / Q000737:chemistry*; D006418:Heme / Q000737:chemistry*; D006735:Horseradish Peroxidase / Q000737:chemistry*; D010084:Oxidation-Reduction
chemical_list: D000975:Antioxidants; D006418:Heme; D045304:Cytochromes c; D006735:Horseradish Peroxidase; D002711:Chloride Peroxidase; D001205:Ascorbic Acid