Peroxidase-like activity of cytochrome b5 is triggered upon hemichrome formation in alkaline pH

Abstract

In alkaline media (pH12) a catalytic peroxidase activity of cytochrome b₅ was found associated to a different conformational state. Upon incubation at this pH, cytochrome b₅ electronic absorption spectrum was altered, with disappearance of characteristic bands of cytochrome b₅ at pH7.0. The appearance of new electronic absorption bands and EPR measurements support the formation of a cytochrome b₅ class B hemichrome with an acquired ability to bind polar ligands. This hemichrome is characterized by a negative formal redox potential and the same folding properties than cytochrome b₅ at pH7. The acquired peroxidase-like activity of cytochrome b₅ found at pH12, driven by a hemichrome formation, suggests a role of this protein in peroxidation products propagation.

Keywords: Alkaline pH; Cytochrome b(5); Hemichromes; Hydrogen peroxide; Low spin state; Peroxidase.