Abstract
A hemin-requiring and streptomycin-resistant mutant of M. pyogenes var. aureus strain SG 511 synthesizes apocatalase if grown in hemin-free media. Resting cell suspensions perform the terminal synthesis of catalase (TSC) upon addition of hemin (ferriprotopor-phyrinchloride). Prolonged treatment of the cells with water or forced aeration causes inactivation of the TSC. This inactivation can be reversed by supplying the cells with various substances during the incubation with hemin. Evidence indicates that Coenzyme A (Co-A) and perhaps a substance derived from glucose in the early steps of glucolysis are indispensable for the TSC. The enhancing effect of anaerobiosis and the inhibiting effect of methylene blue on the TSC are described and the significance of a low oxidation-reduction potential is discussed. The inhibitory effect of p-chloromercuribenzoic acid on TSC which effect is nullified by Co-A and the quantitative relation between these two substances and between Co-A and hemin suggest that Co-A and its corresponding protein perform the TSC by transferring hemin to the apocatalase via formation of an "active hemin," Co-A-S-hemin.