Biochemical and Biophysical Research Communications 2012-03-09

Redox active molecules cytochrome c and vitamin C enhance heme-enzyme peroxidations by serving as non-specific agents for redox relay.

Sudeep Kumar Gade, Subarna Bhattacharya, Kelath Murali Manoj

Index: Biochem. Biophys. Res. Commun. 419(2) , 211-4, (2012)

Full Text: HTML

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.Copyright © 2012 Elsevier Inc. All rights reserved.

Related Compounds

Structure Name/CAS No. Articles
Chloroperoxidase, from Caldariomyces fumago Structure Chloroperoxidase, from Caldariomyces fumago
CAS:9055-20-3