One‐electron reduction of an anthracycline antibiotic carminomycin by a human erythrocyte redox chain

Abstract

Human erythrocyte membranes catalyse the NAD(P)H-dependent generation of the semiquinone of an adriamycin-type antibiotic carminomycin under anaerobic conditions. The maximal yield of the antibiotic radical is about 4-fold higher in the presence of NADPH than of NADH. The possible significance of the antibiotic reduction to the semiquinone by a human erythrocyte membrane redox chain for the clinical usage of these antibiotics is discussed.

Purification and Identification of a Plasma Membrane Associated Electron Transport Protein from Maize (Zea mays L.) Roots

“…Adriamycin has been reported to undergo one electron redox shifts involving paramagnetic species in vivo, associated with anticancer activity in mammalian systems (9). The purified reductase may have reduced adriamycin directly, as erythrocyte membranes were reported to reduce a related anthracycline antibiotic by a pyridine nucleotide-dependent mechanism (20).…”