Affiliation:
1. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710
Abstract
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 μg 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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
353 articles.
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