Lactobacillus plantarum is aerotolerant during log-phase growth on glucose, but is an obligate aerobe on polyols. Respiration was cyanide resistant and under certain conditions was associated with the accumulation of millimolar concentrations of H(2)O(2). On glucose, optimal growth was observed in the absence of O(2). Extracts of L. plantarum did not catalyze the reduction of paraquat by reduced nicotinamide adenine dinucleotide, but plumbagin (5-hydroxy-2-methyl-1,4-naphthoquinone) was readily reduced. Such extracts produced O(2) (-) in the presence of NADH plus plumbagin. Plumbagin caused a 10-fold increase in the rate of respiration of intact cells in the presence of glucose and also imposed a loss of viability which was dependent upon both glucose and O(2). Although extracts of L. plantarum were devoid of true superoxide dismutase activity, this organism was comparable to superoxide dismutase-containing species in its resistance toward hyperbaric O(2) and toward the oxygen-dependent lethality of plumbagin. L. plantarum required Mn-rich media and actively accumulated Mn(II). Soluble extracts were found to contain approximately 9 mug of Mn per mg of protein and 75 to 90% of this Mn was dialyzable. Such extracts exhibited a dialyzable and ethylenediaminetetraacetic acid-inhibitable ability to scavenge O(2) (-). This O(2) (-)-scavenging activity was due to the dialyzable Mn(II) present in these extracts and could be mimicked by MnCl(2). Cells grown in Mn-rich media were enriched in dialyzable Mn and were more resistant toward oxygen toxicity and toward the oxygen-dependent plumbagin toxicity than were cells grown in Mn-deficient media. L. plantarum exhibited no nutritional requirement for iron and little or no iron was present in these cells, even when they were grown in iron-rich media. L. plantarum thus appears to use millimolar levels of Mn(II) to scavenge O(2) (-), much as most other organisms use micromolar levels of superoxide dismutases.

Hydrogen Peroxide↗

PubMed1981

Manganese, superoxide dismutase, and oxygen tolerance in some lactic acid bacteria.

A previous study of the aerotolerant bacterium Lactobacillus plantarum, which lacks superoxide dismutase (SOD), demonstrated that it possesses a novel substitute for this defensive enzyme. Thus, L. plantarum contains 20 to 25 mM Mn(II),m in a dialyzable form, which is able to scavenge O2- apparently as effectively as do the micromolar levels of SOD present in most other organisms. This report describes a survey of the lactic acid bacteria. The substitution of millimolar levels of Mn(II) for micromolar levels of SOD is a common occurrence in this group of microorganisms, which contained either SOD or high levels of Mn(II), but not both. Two strains were found which had neither high levels of Mn(II) nor SOD, and they were, as was expected, very oxygen intolerant. Lactic acid bacteria containing SOD grew better aerobically than anaerobically, whereas the organisms containing Mn(II) in place of SOD showed aerobic growth which was best, at best, equal to anaerobic growth. Plumbagin (5-hydroxy-2-methyl-1,4-naphthoquinone) increases the rate of O2- production in these organisms. Lactobacillus strains containing high intracellular Mn(II) were more resistant to the oxygen-dependent toxicity of plumbagin than were strains containing lower levels of Mn(II). The results support the conclusion that a high internal level of Mn(II) provides these organisms with an important defence against endogenous O2-.

Aerobiosis↗

PubMed1981

The biology of superoxide and of superoxide dismutases - in brief.

Explore the source record for details and available documents.

Catalysis↗

PubMed1981

Chemistry and biochemistry of superoxide dismutases.

The univalent reduction of oxygen to the superoxide radical is a commonplace event in biological systems, and the superoxide dismutases, which catalytically scavenge this radical, are the primary defence against its potential cytotoxicity. The superoxide radical and hydrogen peroxide, can interact to generate the hydroxyl radical. Superoxide dismutases are metalloenzymes that can prevent the generation of hydroxyl radical by keeping the level of superoxide radical vanishingly low. Superoxide dismutases are essential for the survival of all oxygen metabolizing organisms. There are three types of superoxide dismutases: the manganese-containing, the iron-containing, and the copper-zinc-containing superoxide dismutases. The copper-zinc containing superoxide dismutases have generally been isolated from eukaryotic cells except for the enzyme from the symbiotic marine bacterium Photobacterium leiogenthi. The copper-zinc containing superoxide dismutases, from different sources, have a molecular weight of about 32,000, are composed of two identical subunits, and contain one atom of copper and one atom of zinc per subunit. The copper participates in the catalytic activity of the enzyme, while the zinc plays only a structural role. The enzyme has been resolved reversibly. Superoxide dismutases have been seen to provide protection against oxygen toxicity, against compounds that cause exacerbation of oxygen toxicity, against ionizing radiation, and also against the damaging sequelae of prolonged inflammation.

Animals↗

PubMed1980