Oxidation of ascorbic acid with superoxide anion generated by the xanthine-xanthine oxidase system

1975 ◽  
Vol 63 (2) ◽  
pp. 463-468 ◽  
Author(s):  
Morimitsu Nishikimi
Keyword(s):  
Ascorbic Acid ◽  
Xanthine Oxidase ◽  
Superoxide Anion ◽  
Oxidase System

scholarly journals Antioxidant Effects on Lipid Peroxidation by Superoxide of Echinoisoflavanone and Sophoraisoflavanone D from Sophora Chrysophylla Seem

2006 ◽  
Vol 1 (7) ◽  
pp. 1934578X0600100
Author(s):  
Shizuo Toda ◽  
Yoshiaki Shirataki
Keyword(s):  
Lipid Peroxidation ◽  
Xanthine Oxidase ◽  
Superoxide Anion ◽  
Antioxidant Property ◽  
Antioxidant Effect ◽  
Oxidase System ◽  
Antioxidant Effects

The possible antioxidant effect of two isoflavanones, echinoisoflavanone and sophoraisoflavanone D from Sophora chrysophylla Seem. was investigated. Both these compounds inhibited the superoxide anion-mediated lipid peroxidation of lecithin and scavenged superoxide anion generated by the xanthine-xanthine oxidase system. These results indicated the impressive antioxidant property of these two compounds.

scholarly journals A Study of Catechin Photostability Using Photolytic Processing

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 293
Author(s):  
Jeu-Ming P. Yuann ◽  
Shwu-Yuan Lee ◽  
Meei-Ju Yang ◽  
Shiuh-Tsuen Huang ◽  
Chien-Wei Cheng ◽  
...  
Keyword(s):  
Ascorbic Acid ◽  
Superoxide Anion ◽  
Anion Radical ◽  
Alkaline Solutions ◽  
Light Illumination ◽  
Drug Resistant ◽  
Alkaline Ph ◽  
Radical Species ◽  
Alkaline Conditions ◽  
Photolytic Reaction

Catechin exhibits numerous physiological characteristics. In this study, we determined the photosensitivity of catechin to various lights under alkaline conditions, and the mechanisms by which catechin generates free radical species and polymerizes via a photoreaction. In addition to this, the application of catechin photolysis was investigated. A solution of catechin is transparent, but turns yellowish under blue light illumination (BLI) in neutral or weak alkaline solutions. When catechin is subjected to BLI, a dimeric catechin (proanthocyanidin) and a superoxide anion radical (O2•−) are generated in a photolytic reaction. When ascorbic acid or gallic acid is added to catechin and the mixture is subjected to BLI at alkaline pH, fewer catechin dimers and less O2•− are produced, because both acids inhibit the photosensitive oxidation of catechin. When AlCl3 is added to catechin and the mixture is subjected to BLI at pH 8, a photolytic reaction is suppressed by AlCl3, and AlCl3 acts as a catalyst for the disconnection of proanthocyanidin during photolysis. Under alkaline conditions, catechin generates O2•− via photosensitive oxidation, which suppresses the growth of Acinetobacter baumannii (A. baumannii) by at least 4 logs, and deactivates its multi-drug-resistant strain. This study shows that catechin photolysis is a process of oxidation, and that it can be safely applied as a tool for environmental applications.

scholarly journals Bactericidal activity of a superoxide anion-generating system. A model for the polymorphonuclear leukocyte.

1979 ◽  
Vol 149 (1) ◽  
pp. 27-39 ◽  
Author(s):  
H Rosen ◽  
S J Klebanoff
Keyword(s):  
Uric Acid ◽  
Xanthine Oxidase ◽  
Bactericidal Activity ◽  
Parent Strain ◽  
Carotenoid Pigments ◽  
Bacterial Killing ◽  
Oxidase System ◽  
System A ◽  
Presence And Absence ◽  
Generating System

The acetaldehyde-xanthine oxidase system in the presence and absence of myeloperoxidase (MPO) and chloride has been employed as a model of the oxygen-dependent antimicrobial systems of the PMN. The unsupplemented xanthine oxidase system was bactericidal at relatively high acetaldehyde concentrations. The bactericidal activity was inhibited by superoxide dismutase (SOD), catalase, the hydroxyl radical (OH.) scavengers, mannitol and benzoate, the singlet oxygen (1O2) quenchers, azide, histidine, and 1,4-diazabicyclo[2,2,2]octane (DABCO) and by the purines, xanthine, hypoxanthine, and uric acid. The latter effect may account for the relatively weak bactericidal activity of the xanthine oxidase system when purines are employed as substrate. A white, carotenoid-negative mutant strain of Sarcina lutea was more susceptible to the acetaldehyde-xanthine oxidase system than was the yellow, carotenoid-positive parent strain. Carotenoid pigments are potent 1O2 quenchers. The xanthine oxidase system catalyzes the conversion of 2,5-diphenylfuran to cis-dibenzoylethylene, a reaction which can occur by a 1O2 mechanism. This conversion is inhibited by SOD, catalase, azide, histidine, DABCO, xanthine, hypoxanthine, and uric acid but is only slightly inhibited by mannitol and benzoate. The addition of MPO and chloride to the acetaldehyde-xanthine oxidase system greatly increases bactericidal activity; the minimal effective acetaldehyde concentration is decreased 100-fold and the rate and extent of bacterial killing is increased. The bactericidal activity of the MPO-supplemented system is inhibited by catalase, benzoate, azide, DABCO, and histidine but not by SOD or mannitol. Thus, the acetaldehyde-xanthine oxidase system which like phagocytosing PMNs generates superoxide (O.2-) and hydrogen peroxide, is bactericidal both in the presence and absence of MPO and chloride. The MPO-supplemented system is considerably more potent; however, when MPO is absent, bactericidal activity is observed which may be mediated by the interaction of H2O2 and O.2- to form OH. and 1O2.

Topics in Chronic Granulomatous Disease

PEDIATRICS ◽  
1991 ◽  
Vol 88 (1) ◽  
pp. 183-185
Author(s):  
SHIGENOBU UMEKI
Keyword(s):  
Nadph Oxidase ◽  
Chronic Granulomatous Disease ◽  
Host Defense ◽  
Superoxide Anion ◽  
Fungal Infections ◽  
Regulatory Elements ◽  
Granulomatous Disease ◽  
Phagocytic Cells ◽  
Oxidase System ◽  
Membrane Bound

To the Editor.— Such phagocytic cells as neutrophils and macrophages are crucial elements in the host defense against bacterial [See table in the PDF file] and fungal infections. Microbicidal activity depends to a large extent on NADPH oxidase system, which can be activated by stimuli (bacteria, fungi) and which generates the superoxide anion and other highly reactive forms of reduced oxygen.1,2 The neutrophil NADPH oxidase system is composed functionally of membrane-bound catalytic components (which consist of at least two constituents, the low potential cytochrome b5583-5 and flavoprotein5) and soluble cytosolic components6,7 which participate as either catalytic or regulatory elements.

Hyperoxia and self- or neutrophil-generated O2 metabolites inactivate xanthine oxidase

1988 ◽  
Vol 65 (5) ◽  
pp. 2349-2353 ◽  
Author(s):  
L. S. Terada ◽  
C. J. Beehler ◽  
A. Banerjee ◽  
J. M. Brown ◽  
M. A. Grosso ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Xanthine Oxidase ◽  
Superoxide Anion ◽  
Hypochlorous Acid ◽  
Control Mechanism ◽  
Xanthine Dehydrogenase ◽  
Biological Processes ◽  
Lung Endothelial Cells ◽  
Cellular Control

Xanthine oxidase (XO) and xanthine dehydrogenase (XD) activities decreased in lungs isolated from rats and cultured lung endothelial cells that had been exposed to hyperoxia. Purified XO activity also decreased after addition of a variety of chemically generated O2 metabolite species (superoxide anion, hydrogen peroxide, hydroxyl radical, or hypochlorous acid), hypoxanthine, or stimulated neutrophils in vitro. XO inactivation by chemically, self-, or neutrophil-generated O2 metabolites was decreased by simultaneous addition of various O2 metabolite scavengers but not their inactive analogues. Since XO appears to contribute to a variety of biological processes and diseases, hyperoxia- or O2 metabolite-mediated decreases in XO activity may be an important cellular control mechanism.

scholarly journals The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin

1988 ◽  
Vol 256 (3) ◽  
pp. 923-928 ◽  
Author(s):  
H P Monteiro ◽  
C C Winterbourn
Keyword(s):  
Lipid Peroxidation ◽  
Free Radicals ◽  
Xanthine Oxidase ◽  
Binding Protein ◽  
Gel Filtration ◽  
Iron Binding ◽  
Oxidase System ◽  
Oxidative Reactions ◽  
Phospholipid Liposomes ◽  
Iron Binding Protein

By the use of gel filtration and [59Fe]ferritin, apotransferrin and apolactoferrin were shown to take up iron released from ferritin by superoxide generated by hypoxanthine and xanthine oxidase. Apotransferrin also inhibited uptake of released iron by ferrozine. Ferritin and the xanthine oxidase system induced lipid peroxidation in phospholipid liposomes. This peroxidation was inhibited by apotransferrin or apolactoferrin. Thus, although superoxide and other free radicals can release iron from ferritin, either iron-binding protein, if present, should take up this iron and prevent its catalysing subsequent oxidative reactions.

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