2002
DOI: 10.1046/j.1365-2958.2002.02719.x
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A potential role for periplasmic superoxide dismutase in blocking the penetration of external superoxide into the cytosol of Gram‐negative bacteria

Abstract: , [95][96][97][98][99][100][101][102][103][104][105][106]

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Cited by 144 publications
(130 citation statements)
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“…1B). Given the short half-life of superoxide and its low membrane permeability (reviewed by Korshunov and Imlay, 2002) it is more likely that the superoxide measured in this assay is generated at the plasma membrane.…”
Section: Resultsmentioning
confidence: 99%
“…1B). Given the short half-life of superoxide and its low membrane permeability (reviewed by Korshunov and Imlay, 2002) it is more likely that the superoxide measured in this assay is generated at the plasma membrane.…”
Section: Resultsmentioning
confidence: 99%
“…As this radical is neutral, it is capable of passing through the cell membranes easily and is considered to have better sterilizing effects than the O2 − • radical 22) . O2 − • and HOO• are thought to be in equilibrium as shown in the following equation 22) .…”
Section: Ros Inhibition Testmentioning
confidence: 99%
“…These two sets of results are fully consistent with each other and indicate that NOX activity produces only a small fraction of O 2 ⅐ Ϫ produced by the muscle fiber and, therefore, compared with mitochondria, the plasma membrane NOX activity is not a major source of O 2 ⅐ Ϫ production. Although the mechanism by which some O 2 ⅐ Ϫ crosses the mitochondrial and plasma membranes in skeletal muscles is not clear, O 2 ⅐ Ϫ is in rapid equilibrium with its protonated and uncharged form (⅐OOH) (about 1% of total O 2 ⅐ Ϫ at pH 7) that can readily cross membranes (10). Considering that the pH in the intermembrane space is more acidic than that in the surrounding environment, this would increase the fraction of protonated O 2 ⅐ Ϫ , facilitating its diffusion across the outer mitochondrial membrane.…”
mentioning
confidence: 99%