Oxidation of formate by mycobacteria of the scrofulaceum group.

Intact cells obtained from Mycobacterium scrofulaceum as well as from mycobacterial strains M.A6 and M.R56 isolated respectively from leprous tissues of armadillo and rat leproma and grown with glycerol as the oxidizable substrate catalyzed complete oxidation of formate. The stoichiometry of formate oxidase system yielded a value of 2 mol of CO2 produced per mole of O2 or per 2 moles of formate consumed. Cell-free preparations from these three strains of mycobacteria contained formate dehydrogenase which was associated exclusively in the particulate fraction. Formate oxidation was markedly stimulated by small amounts of selenite and molybdate added together. Formate-reduced minus oxidized difference spectra disclosed cytochromes of the b type while spectral evidence did not suggest the existence of cytochromes a or c components. The effect of 2-N-heptyl-4-hydroxyquinoline-N-oxide on the redox state of cytochromes indicated that formate oxidation was mediated by cytochrome b with absorption maximum of 556 nm and not of 562 nm.