scholarly journals Hydroxylation of p-coumaric acid by horseradish peroxidase. The role of superoxide and hydroxyl radicals

1976 ◽  
Vol 153 (3) ◽  
pp. 513-518 ◽  
Author(s):  
B Halliwell ◽  
S Ahluwalia
Keyword(s):  
Superoxide Dismutase ◽  
Horseradish Peroxidase ◽  
Caffeic Acid ◽  
Hydroxyl Radicals ◽  
Superoxide Radical ◽  
Coumaric Acid ◽  
Low Concentrations ◽  
Superoxide Dismutase 3 ◽  
Superoxide Dismutase 2

1. In the presence of dihydroxyfumarate, horseradish peroxidase catalyses the conversion of p-coumaric acid into caffeic acid at pH 6. This hydroxylation is completely inhibited by superoxide dismutase. 2. Dihydroxyfumarate cannot be replaced by ascorbate H2O2, NADH, cysteine or sulphite. Peroxidase can be replaced by high (10 mM) concentrations of FeSO4, but this reaction is almost unaffected by superoxide dismutase. 3. Hydroxylation by the peroxidase/dihydroxyfumarate system is completely inhibited by low concentrations of Mn2+ or Cu2+. It is proposed that this is due to the ability of these metal ions to react with the superoxide radical O2–. 4. Hydroxylation is partially inhibited by mannitol, Tris or ethanol and completely inhibited by formate. This seems to be due to the ability of these reagents to react with the hydroxyl radical -OH. 5. It is concluded that O2– is generated during the oxidation of dihydroxyfumarate by peroxidase and reacts with H2O2 to produce hydroxyl radicals, which then convert p-coumaric acid into caffeic acid.

scholarly journals Scavenging of oxygen radicals by heme peroxidases.

1996 ◽  
Vol 43 (4) ◽  
pp. 673-678 ◽  
Author(s):  
L Gebicka ◽  
J L Gebicki
Keyword(s):  
Horseradish Peroxidase ◽  
Hydroxyl Radicals ◽  
Superoxide Radical ◽  
Cation Radical ◽  
Compound I ◽  
Superoxide Radical Anion ◽  
Form Compound ◽  
Activity Loss ◽  
Heme Peroxidases ◽  
Compound Ii

The reactions of two heme peroxidases, horseradish peroxidase and lactoperoxidase and their compounds II (oxoferryl heme intermediates, Fe(IV) = O or ferric protein radical Fe(III)R.) and compounds III (resonance hybrids [Fe(III)-O2-. Fe(II)-O2] with superoxide radical anion generated enzymatically or radiolytically, and with hydroxyl radicals generated radiolytically, were investigated. It is suggested that only the protein radical form of compound II of lactoperoxidase reacts with superoxide, whereas compound II of horseradish peroxidase, which exists only in oxoferryl form, is unreactive towards superoxide. Compound III of the investigated peroxidases does not react with superoxide. The lactoperoxidase activity loss induced by hydroxyl radicals is closely related to the loss of the ability to form compound I (oxoferryl porphyrin pi-cation radical, Fe(IV) = O(Por+.) or oxoferryl protein radical Fe(IV) = O(R.)). On the other hand, the modification of horseradish peroxidase induced by hydroxyl radicals has been reported to cause also restrictions in substrate binding (Gebicka, L. & Gebicki, J.L., 1996, Biochimie 78, 62-65). Nevertheless, it has been found that only a small fraction of hydroxyl radicals generated homogeneously does inactivate the enzymes.

scholarly journals UV-Vis Spectroelectrochemistry of Oleuropein, Tyrosol, and p-Coumaric Acid Individually and in an Equimolar Combination. Differences in LC-ESI-MS2 Profiles of Oxidation Products and Their Neuroprotective Properties

Biomolecules ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 802 ◽  
Author(s):  
Morgane Lambert de Malezieu ◽  
Solenn Ferron ◽  
Aurélie Sauvager ◽  
Patricia Courtel ◽  
Charles Ramassamy ◽  
...  
Keyword(s):  
Neuronal Death ◽  
Oxidation Products ◽  
Coumaric Acid ◽  
Low Concentrations ◽  
Relevant Role ◽  
Electron Transfer Properties ◽  
Transfer Properties ◽  
Oxidized Products

Major phenolic compounds from olive oil (ArOH-EVOO), oleuropein (Ole), tyrosol (Tyr), and p-coumaric acid (p-Cou), are known for their antioxidant and neuroprotective properties. We previously demonstrated that their combination could potentiate their antioxidant activity in vitro and in cellulo. To further our knowledge of their electron-transfer properties, Ole, Tyr, and p-Cou underwent a spectroelectrochemical study, performed either individually or in equimolar mixtures. Two mixtures (Mix and Mix-seq) were prepared in order to determine whether distinct molecules could arise from their simultaneous or sequential oxidation. The comparison of Liquid Chromatography–Electrospray Ionization–Tandem Mass Spectrometry (LC-ESI-MS2) profiles highlighted the presence of specific oxidized products found in the mixes. We hypothesized that they derived from the dimerization between Tyr and Ole or p-Cou, which have reacted either in their native or oxidized forms. Moreover, Ole regenerates when the Mix undergoes oxidation. Our study also showed significant neuroprotection by oxidized Ole and oxidized Mix against H2O2 toxicity on SK-N-SH cells, after 24 h of treatment with very low concentrations (1 and 5 nM). This suggests the putative relevant role of oxidized Ole products to protect or delay neuronal death.

Tempeh extract reduces cellular ROS levels and upregulates the expression of antioxidant enzymes

Food Research ◽  
2021 ◽  
Vol 5 (3) ◽  
pp. 121-128
Author(s):  
R. Surya ◽  
A. Romulo ◽  
Y. Suryani
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Enzymes ◽  
Antioxidant Activities ◽  
Ethanol Extract ◽  
Soybean Extract ◽  
Cellular Reactive Oxygen Species ◽  
Superoxide Dismutase 3 ◽  
Insight Into ◽  
Superoxide Dismutase 2

Tempeh is an Indonesian traditional food produced from soybeans through a mould fermentation involving Rhizopus oligosporus. It is rich in bioactive phytochemicals, including isoflavones that are known to exhibit antioxidant activities. This study aimed to investigate the ability of tempeh ethanol extract to reduce cellular reactive oxygen species (ROS) levels in HepG2 cells in vitro. Tempeh extract exhibited greater total phenolics, total flavonoids and free radical inhibition capacity than soybean extract. Both tempeh extract and soybean extract reduced the basal levels of cellular ROS in the cells, but tempeh extract induced higher expression of antioxidant enzymes [catalase, superoxide dismutase-2 (SOD2) and superoxide dismutase-3 (SOD3)] compared to soybean extract. This study provides novel evidence suggesting the ability of tempeh to tackle cellular oxidative stress by upregulating the expression of antioxidant enzymes. These findings would give an insight into the potential of tempeh to be developed as a functional food beneficial for human health.

Catalytic role of iron-superoxide dismutase in hydrogen abstraction by super oxide radical anion from ascorbic acid

RSC Advances ◽  
2016 ◽  
Vol 6 (89) ◽  
pp. 86650-86662 ◽  
Author(s):  
Manish K. Tiwari ◽  
Phool C. Mishra
Keyword(s):  
Ascorbic Acid ◽  
Superoxide Dismutase ◽  
Active Site ◽  
Radical Anion ◽  
Superoxide Radical ◽  
Hydrogen Abstraction ◽  
Iron Superoxide Dismutase ◽  
Superoxide Radical Anion ◽  
Catalytic Role

The catalytic role of iron-superoxide dismutase (Fe-SOD) in the working of ascorbic acid (AA) as a superoxide radical anion scavenger has been studied by employing a model developed recently for the active site of the enzyme.

scholarly journals Cardiovascular Mitochondrial Dysfunction Induced by Cocaine: Biomarkers and Possible Beneficial Effects of Modulators of Oxidative Stress

2017 ◽  
Vol 2017 ◽  
pp. 1-15 ◽  
Author(s):  
Manuela Graziani ◽  
Paolo Sarti ◽  
Marzia Arese ◽  
Maria Chiara Magnifico ◽  
Aldo Badiani ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Superoxide Dismutase ◽  
Mitochondrial Dysfunction ◽  
Cocaine Abuse ◽  
Biological Marker ◽  
Cardiovascular Toxicity ◽  
Beneficial Effects ◽  
Potential Use ◽  
Superoxide Dismutase 2

Cocaine abuse has long been known to cause morbidity and mortality due to its cardiovascular toxic effects. The pathogenesis of the cardiovascular toxicity of cocaine use has been largely reviewed, and the most recent data indicate a fundamental role of oxidative stress in cocaine-induced cardiovascular toxicity, indicating that mitochondrial dysfunction is involved in the mechanisms of oxidative stress. The comprehension of the mechanisms involving mitochondrial dysfunction could help in selecting the most appropriate mitochondria injury biological marker, such as superoxide dismutase-2 activity and glutathionylated hemoglobin. The potential use of modulators of oxidative stress (mitoubiquinone, the short-chain quinone idebenone, and allopurinol) in the treatment of cocaine cardiotoxic effects is also suggested to promote further investigations on these potential mitochondria-targeted antioxidant strategies.

scholarly journals Generation of hydrogen peroxide, superoxide and hydroxyl radicals during the oxidation of dihydroxyfumaric acid by peroxidase

1977 ◽  
Vol 163 (3) ◽  
pp. 441-448 ◽  
Author(s):  
B Halliwell
Keyword(s):  
Hydrogen Peroxide ◽  
Superoxide Dismutase ◽  
Hydroxyl Radicals ◽  
Coumaric Acid ◽  
Enzymic Oxidation ◽  
Enzymic Reaction ◽  
Low Rate

1. Dihydroxyfumarate slowly autoxidizes at pH6. This reaction is inhibited by superoxide dismutase but not by EDTA. Mn2+ catalyses dihydroxyfumarate oxidation by reacting with O2 leads to to form Mn3+, which seems to oxidize dihydrofumarate rapidly. Cu2+ also catalyses dihydroxyfumarate oxidation, but by a mechanism that does not involve O2 leads to. 2. Peroxidase catalyses oxidation of dihydroxyfumarate at pH6; addition of H2O2 does not increase the rate. Experiments with superoxide dismutase and catalase suggest that there are two types of oxidation taking place: an enzymic, H2O2-dependent oxidation of dihydroxyfumarate by peroxidase, and a non-enzymic reaction involving oxidation of dihydroxyfumarate by O2 leads to. The latter accounts for most of the observed oxidation of dihydroxyfumarate. 3. During dihydroxyfumarate oxidation, most peroxidase is present as compound III, and the enzymic oxidation may be limited by the low rate of breakdown of this compound. 4. Addition of p-coumaric acid to the peroxidase/dihydroxyfumarate system increases the rate of dihydroxyfumarate oxidation, which is now stimulated by addition of H2O2, and is more sensitive to inhibition by catalase but less sensitive to superoxide dismutase. Compound III is decomposed in the presence of p-coumaric acid. p-Hydroxybenzoate has similar, but much smaller, effects on dihydroxyfumarate oxidation. However, salicylate affects neither the rate nor the mechanism of dihydroxyfumarate oxidation. 5. p-Hydroxybenzoate, salicylate and p-coumarate are hydroxylated by the peroxidase/dihydroxyfumarate system. Experiments using scavengers of hydroxyl radicals shown that OH is required. Ability to increase dihydroxyfumarate oxidation is not necessary for hydroxylation to occur.

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