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Volumn 2, Issue 2, 1998, Pages 253-262

The dark side of dioxygen biochemistry

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[No Author keywords available]

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JANUS;

EID: 0032042992     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80067-7     Document Type: Article
Times cited : (188)

References (86)
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    • The copper- And zinc-containing superoxide dismutase from Escherichia coli: Molecular weight and stability
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    • In this paper the authors showed that a specific protein carrier of copper, Lys7p, was required for the proper metallation of CuZnSOD in Saccharomyces cerevisiae. A lys7 knockout strain showed an oxygen sensitive phenotype characteristic of CuZnSOD deficiency. This strain contained copper-deficient CuZnSOD protein but showed normal processing of other copper proteins. The oxygen sensitivity of the lys7 knockout strain is particularly striking since both the CuZnSOD protein and the copper ions are present in sufficient amounts but the copper is not inserted into the protein
    • Culotta VC, Klomp LW, Strain J, Casareno RL, Krems B, Gitlin JD: The copper chaperone for superoxide dismutase. J Biol Chem 1997, 272:23469-23472. In this paper the authors showed that a specific protein carrier of copper, Lys7p, was required for the proper metallation of CuZnSOD in Saccharomyces cerevisiae. A lys7 knockout strain showed an oxygen sensitive phenotype characteristic of CuZnSOD deficiency. This strain contained copper-deficient CuZnSOD protein but showed normal processing of other copper proteins. The oxygen sensitivity of the lys7 knockout strain is particularly striking since both the CuZnSOD protein and the copper ions are present in sufficient amounts but the copper is not inserted into the protein.
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    • A potent superoxide dismutase mimic: Manganese β-octabromo-mesotetrakis-(N-methylpyridinium-4-yl) porphyrin
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    • Weiss RH, Fretland DJ, Baron DA, Ryan US, Riley DP: Manganese-based superoxide dismutase mimetics inhibit neutrophil infiltration in vivo. J Biol Chem 1996, 271:26149-26156. This paper describes in vivo studies of several manganese-containing synthetic SODs which had previously been shown to have high SOD activity and to inhibit neutrophil-mediated cell injury in vitro. These drugs were found to inhibit colonic tissue injury and neutrophil accumulation in a dose-dependent manner. Similar manganese-containing compounds with little or no SOD activity were ineffective. These results support a proinflammatory role for superoxide in tissue injury and provide further encouragement for development of synthetic SODs as drugs.
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    • This paper reports identification and characterization of the enzyme methionine sulfoxide reductase (MsrA) in the yeast S. cerevisiae. Interruption of the yeast gene resulted in a null mutant, which totally lost its cellular MsrA activity and was more susceptible to oxidative stress than its wild type parent strain. Under various oxidative stresses, high levels of free and protein-bound methionine sulfoxide were found in extracts of the null mutant cells relative to their wild type parent cells. These results suggest that methionine plus MsrA constitutes an antioxidant system in which free or external methionine residues act as scavengers of reactive oxygen species followed by re-reduction of the resulting methionine residues in a reaction catalyzed by MsrA. MsrA should thus be added to the list of antioxidant enzymes in the cell
    • Moskovitz J, Berlett BS, Poston JM, Stadtman ER: The yeast peptide-methionine sulfoxide reductase functions as an antioxidant in vivo. Proc Natl Acad Sci USA 1997, 94:9585-9589. This paper reports identification and characterization of the enzyme methionine sulfoxide reductase (MsrA) in the yeast S. cerevisiae. Interruption of the yeast gene resulted in a null mutant, which totally lost its cellular MsrA activity and was more susceptible to oxidative stress than its wild type parent strain. Under various oxidative stresses, high levels of free and protein-bound methionine sulfoxide were found in extracts of the null mutant cells relative to their wild type parent cells. These results suggest that methionine plus MsrA constitutes an antioxidant system in which free or external methionine residues act as scavengers of reactive oxygen species followed by re-reduction of the resulting methionine residues in a reaction catalyzed by MsrA. MsrA should thus be added to the list of antioxidant enzymes in the cell.
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    • This paper addresses the issue of whether the susceptibility to oxidative damage of individual amino acid residues in proteins depends upon the secondary structure in which they occur. Ab initio calculations indicated that amino acid residues in β sheet structures would be more susceptible to hydrogen atom abstraction at the α-carbon position relative to those in α-helical structures. Theoretical calculations also indicated that sensitivity increases in the series alanine
    • Rauk A, Yu D, Armstrong DA: Toward site specificity of oxidative damage in proteins: C-H and C-C bond dissociation energies and reduction potentials of the radicals of alanine, serine, and threonine residues - an ab initio study. J Am Chem Soc 1997, 119:208-217. This paper addresses the issue of whether the susceptibility to oxidative damage of individual amino acid residues in proteins depends upon the secondary structure in which they occur. Ab initio calculations indicated that amino acid residues in β sheet structures would be more susceptible to hydrogen atom abstraction at the α-carbon position relative to those in α-helical structures. Theoretical calculations also indicated that sensitivity increases in the series alanine
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    • Differences in the regulation of iron regulatory protein-1 (IRP-1) by extra- And intracellular oxidative stress
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    • Prooxidant-initiated lipid peroxidation in isolated rat hepatocytes: Detection of 4-hydroxynonenal- And malondialdehyde-protein adducts
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    • 4 nor iron/ascorbate elicited changes in 4-HNE or induced 4-HNE-modified proteins. Experiments of the type described in this paper will be very useful in establishing the details of oxidative damage pathways occurring in vivo.
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    • Metabolic activation of trans-4-hydroxy-2-nonenal, a toxic product of membrane lipid peroxidation and inhibitor of P450 cytochromes
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    • Iron homeostasis, oxidative stress, and DNA damage
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    • Site-specific DNA damage induced by NADH in the presence of copper(II): Role of active oxygen species
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    • Oxidative damage and tyrosine nitration from peroxynitrite
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    • Beckman JS: Oxidative damage and tyrosine nitration from peroxynitrite. Chem Res Toxicol 1996, 9:836-844. Peroxynitrite, formed from the reaction of nitric oxide (NO) with superoxide, has been implicated as a major agent of NO-induced cytotoxicity. This comprehensive review describes the experiments in support of this hypothesis.
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    • -OONO) play a major role in cytotoxicity? Accounts Chem Res 1997, 30:149-152. This commentary critically evaluates the hypothesis that peroxynitrite plays a major role in cytotoxicity in vivo and concludes that the evidence currently available is not sufficient to reach that conclusion.
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    • Halliwell B: What nitrates tyrosine? Is nitrotyrosine specific as a biomarker of peroxynitrite formation in vivo? FEBS Lett 1997, 411:157-160. This paper concludes that the evidence is not conclusive that nitrotyrosine is specific as a biomarker of peroxynitrite formation in vivo and suggests that the nitrating agent be referred to as a reactive nitrogen species.
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    • Carbon dioxide: Physiological catalyst for peroxynitrite-mediated cellular damage or cellular protectant?
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    • -. This reaction occurs at physiologically relevant concentrations and may represent the major fate of peroxynitrite when it is formed in vivo. This paper reviews this topic and concludes that considerably more knowledge about the lifetime and reactivity of this adduct is required before its biological significance can be assessed.
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    • Inhibition of the catalytic activity of alcohol dehydrogenase by nitric oxide is associated with S-nitrosylation and the release of zinc
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    • ras interaction
    • Nitric oxide (NO) stimulates Ras by increasing its guanine nucleotide exchange activity by nitrosothiol formation. In this report the authors determine that this S-nitrosylation specifically occurs at Cys118 of the protein. Mutation of this residue to a serine prevents NO induction of guanine nucleotide exchange and two mitogen-activated protein (MAP) kinases downstream of Ras
    • ras interaction. J Biol Chem 1997, 272:4323-4326. Nitric oxide (NO) stimulates Ras by increasing its guanine nucleotide exchange activity by nitrosothiol formation. In this report the authors determine that this S-nitrosylation specifically occurs at Cys118 of the protein. Mutation of this residue to a serine prevents NO induction of guanine nucleotide exchange and two mitogen-activated protein (MAP) kinases downstream of Ras.
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    • A novel reaction mechanism for the formation of S-nitrosothiol in vivo
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    • 2 to give RS-N=O plus superoxide. Chemical evidence in support of the feasibility of this mechanism is presented.
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    • Reactive oxygen species and Alzheimer's disease
    • This commentary describes evidence suggesting that the presence of amyloid peptide βA4, which is derived from the amyloid precursor protein (APP), leads to oxidative stress by a mechanism that involves complexation and reduction of Cu(II) to Cu(I). The paper is marred by the failure of the authors to address satisfactorily earlier criticisms of the use of bathocuprein as a method for detection of Cu(I) formation [76]
    • Multhaup G, Ruppert T, Schlicksupp A, Hesse L, Beher D, Masters CL, Beyreuther K: Reactive oxygen species and Alzheimer's disease. Biochem Pharmacol 1997, 54:533-539. This commentary describes evidence suggesting that the presence of amyloid peptide βA4, which is derived from the amyloid precursor protein (APP), leads to oxidative stress by a mechanism that involves complexation and reduction of Cu(II) to Cu(I). The paper is marred by the failure of the authors to address satisfactorily earlier criticisms of the use of bathocuprein as a method for detection of Cu(I) formation [76].
    • (1997) Biochem Pharmacol , vol.54 , pp. 533-539
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    • Mechanisms of neurotoxicity associated with amyloid βdeposition and the role of free radicals in the pathogenesis of Alzheimer's disease: A critical appraisal
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    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
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    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • Friedreich ataxia is a degenerative disease linked to mutations in the frataxin gene. This gene is believed to be involved in mitochondrial iron transport, based on studies of a homologous protein in yeast. In this report, the authors show that the activities of aconitase and complexes I, II, and III of the electron transport chain, which are Fe-S cluster containing enzymes, are reduced in heart tissue from two Freidreich ataxia patients relative to the average control activities
    • Rotig A, de Lonlay P, Chretien D, Foury F, Koenig M, Sidi D, Munnich A, Rustin P: Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat Genet 1997, 17:215-217. Friedreich ataxia is a degenerative disease linked to mutations in the frataxin gene. This gene is believed to be involved in mitochondrial iron transport, based on studies of a homologous protein in yeast. In this report, the authors show that the activities of aconitase and complexes I, II, and III of the electron transport chain, which are Fe-S cluster containing enzymes, are reduced in heart tissue from two Freidreich ataxia patients relative to the average control activities.
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    • Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis
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