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.
