The Role of Superoxide in the Induction of Superoxide Dismutase and Oxygen Toxicity

Fee, James A.; Lees, Alison C.; Bloch, P L; Neidhardt, Frederick C.

doi:10.1016/b978-0-12-164380-5.50041-4

Cited by 10 publications

(11 citation statements)

References 27 publications

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“…Thus, by analogy with previous results (Boehme et al, 1976;Brown and Yein, 1978;Seither and Brown, 1982;Fee et al, 1979Fee et al, , 1980Heitkamp and Brown, 1981), the requirements for specific amino acids to prevent growth inhibition and induction of stringency by paraquat and nitrofurantoin indicate a block(s) in the biosynthetic pathways of these specific amino acids by these agents. Nitrofurantoin, in contrast to paraquat and hyperoxia, only blocks the synthesis of the branched-chain amino acids.…”

Section: Discussionsupporting

confidence: 78%

“…2). Ten specific amino acids, whose individual and composite omission from the complete set of 20 amino acids resulted in a statistically significant decrease in growth rate in hyperbaric oxygen (Boehme et al, 1976) and that produced a similar effect in paraquat poisoned cells (Fee et al, 1979), were added to cultures poisoned by paraquat. Addition of these 10 amino acids resulted in an abrupt restoration of growth (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…This response, reviewed by Cashel (1975), results from amino acid starvation and is mediated by a rapid increase in the intracellular concentration of guanosine 5'-d1phosphate 3'-d1phosphate (ppGpp), which is a regulator of many cellular biosynthetic processes in prokaryotes (Gallant, 1979). We measured the intracellular concentrations of ppGpp in E. coli treated with paraquat and nitrofurantoin under several nutritional states with respect to amino acids, because we had previously discovered that hyperbaric oxygen poisons specific amino acid biosynthetic pathways (Boehme et al, 1976;Brown and Yein, 1978) and induces stringency (Seither and Brown, 1982), and because the mechanisms of toxicity of paraquat and hyperbaric oxygen have been found to share other important similarities Fee et al, 1980;Brown and Song, 1980;Heitkamp and Brown, 1981), including significant circumvention of growth inhibition by specific amino acids (Boehme et al, 1976;Fee et al, 1979).…”

Section: Introductionmentioning

confidence: 99%

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Paraquat and nitrofurantoin inhibit growth ofescherichia coliby inducing stringency

Seither

Brown

1984

Journal of Toxicology and Environmental Health

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The herbicide paraquat and the antibiotic nitrofurantoin (redox-active compounds that can transfer electrons singly to oxygen) induced intracellular accumulation of the regulatory inhibitor guanosine tetraphosphate (stringency) in Escherichia coli. This mechanism is sufficient to account for the rapid bacteristasis produced in minimal medium by these agents. The growth inhibition and stringency induction were prevented by inclusion of specific amino acids in the medium. Stringency was first reported to result from amino acid starvation, with unloaded transfer ribonucleic acids (tRNAs) acting as the trigger. Previously, inhibition of growth of E. coli by paraquat and hyperbaric oxygen were shown to be prevented by inclusion in the medium of a nearly identical profile of specific amino acids, including branched-chain amino acids, which were required because of poisoning of their biosynthesis at the dihydroxyacid dehydratase site, and stringency has been induced by hyperbaric oxygen poisoning. Thus, stringency induction via a common poisoned site in branched-chain amino acid biosynthesis appears to be a shared mechanism of toxicity for these agents and hyperbaric oxygen, which also share the propensity for one-electron-transfer, free-radical reactions in cells.

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Section: Discussionsupporting

confidence: 78%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Paraquat and nitrofurantoin inhibit growth ofescherichia coliby inducing stringency

Seither

Brown

1984

Journal of Toxicology and Environmental Health

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“…Doubts have been expressed, however, concerning the true function of this protein owing to the absence of a chemical explanation for the source of the proposed toxicity of siperoxide (30)(31)(32)(33). If dismutation of superoxide is not the primary function of this protein, one is led to consider alternative functions.…”

Section: Discussionmentioning

confidence: 99%

pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase

Valentine

Pantoliano

McDonnell

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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Bovine erythrocyte superoxide dismutase (Cu2Zn2SODase; superoxide:superoxide oxidoreductase, EC 1.15.1.1) consists of two identical subunits each containing Cu2+ and Zn2+ in close proximity. We describe here electron spin resonance (ESR) and visible absorption spectroscopic studies of the zinc-free derivative of this protein, Cu2E2SODase (E = empty) over the pH range 6-10. The ESR spectrum of the zincfree protein at 77 K is markedly pH dependent. At pH < 8.0 the ESR spectrum is axial in appearance. At pH > 8.0, the lineshape becomes increasingly distorted with increasing pH until, at pH = 9.5, the spectrum is very broad and resembles that of the four-copper derivative Cu2Cu2SODase and of model imidazolate-bridged binuclear Cu(II) complexes. ESR spectra at 30°C are also consistent with formation of Cu(II)Im-Cu(II). A plot of changes in the signal amplitude of g1 for Cu2E2SODase as a function of pH gives an apparent pKa of 8.2 for the transition. The long-wavelength absorption with Xmax = 700 nm characteristic of Cu2E2SODase shifts with increasing pH to 800 nm and the resulting visible spectrum is identical to that of Cu2-Cu2SODase. All of the above-mentioned spectroscopic changes induced by additions of NaOH are reversed when the pH is decreased with HNO3, although the approach to equilibrium is slow in the latter case. The results of these experiments are consistent with a reversible, pH-dependent migration of Cu2+ from the native copper site of one subunit of the zinc-free protein to the empty zinc site of another subunit. By contrast, native protein, Cu2Zn2SODase, and the four-copper protein, Cu2-Cu2SODase, show no variation in visible or ESR spectral properties in this pH range. Some previous results concerning the activity of Cu2E2SODase and its thermal stability are reexamined in light of these new findings.

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“…Inhibition of SOD could favor high concentrations of O^". Al though its chemical reactivity is limited, O?-can react with H2O2 to form the highly toxic free hydroxyl radical (OH') following a Haber-Weiss reaction, catalyzed by traces of me tal [12], The OH" radical may directly affect lipids and proteins, including those of the electron transport system. On the other hand, OH' is metabolized by glutathione reductase by which NADPH is oxidized.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of Superoxide Dismutase from Ascaris suum by Benzimidazoles and Synthesized Pyrimidine and Glycine Derivatives

Sánchez‐Moreno

Entrala²,

Janssen³

et al. 1996

Pharmacology

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Copper-zinc superoxide dismutase was purified from Ascαris suum (Nematoda). Four benzimidazole derivatives, six recently synthesized pyrimidine derivatives and eleven recently synthesized glycine derivatives were shown to inhibit: (1) purified extracts of A. suum superoxide dismutase; (2) superoxide dismutase from host liver, and (3) purified extracts of superoxide dismutase from living A. suum incubated in the presence of these drugs. Thiabendazole compounds, with a documented effect against helminth parasites, were found to affect the superoxide dismutase. The inhibitory effects of some pyrimidine and glycine derivatives were higher than those of benzimidazoles, and the pyrimidine compounds failed to inhibit the host’s enzyme. These derivatives are candidate anthelmintics, acting as inhibitors of certain metalloenzymes in parasites.

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The Role of Superoxide in the Induction of Superoxide Dismutase and Oxygen Toxicity

Cited by 10 publications

References 27 publications

Paraquat and nitrofurantoin inhibit growth ofescherichia coliby inducing stringency

Paraquat and nitrofurantoin inhibit growth ofescherichia coliby inducing stringency

pH-dependent migration of copper(II) to the vacant zinc-binding site of zinc-free bovine erythrocyte superoxide dismutase

Inhibition of Superoxide Dismutase from Ascaris suum by Benzimidazoles and Synthesized Pyrimidine and Glycine Derivatives

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