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PubMed2005

Nitric oxide and hydrogen peroxide in tomato resistance. Nitric oxide modulates hydrogen peroxide level in o-hydroxyethylorutin-induced resistance to Botrytis cinerea in tomato.

Nitric oxide (NO) has been postulated to be required, together with reactive oxygen species (ROS), for activation of disease resistance reactions of plants to infection with a pathogen or elicitor treatment. However, biochemical mechanisms by which ROS and NO participate in these reactions are still under intensive study and controversial debate. We previously demonstrated that o-hydroxyethylorutin when applied on tomato leaves (Lycopersicon esculentum Mill. cv. "Perkoz") restricted Botrytis cinerea infection development. In this research we investigated ROS and NO generation in tomato plants treated with o-hydroxyethylorutin, non-treated and infected ones. The NO content was enhanced or decreased in the studied plants by supplying them with NO generator-SNP or scavenger-cPTIO. NO detection was carried out using diaminofluorescein diacetate (DAF-DA) in conjunction with confocal laser scanning microscopy. The influence of elevated and decreased levels of NO on B. cinerea infection development and ROS generation was studied. The elevated NO concentration in tomato leaves strongly decreased hydrogen peroxide concentration without affecting other studied ROS (superoxide anion and hydroxyl radical) levels. H2O2 concentrations in NO-supplied leaves were low regardless of further treatment of tomato leaves with o-hydroxyethylorutin or inoculation with B. cinerea. The low H2O2 concentration coincided with quick and severe infection development in NO-supplied leaves. As activities of enzymes generating (SOD EC 1.15.1.1)) and removing (APX EC 1.11.1.11, CAT EC 1.11.1.6) H2O2 were unchanged in the studied plants, the decrease in H2O2 concentration was probably due to a direct NO-H2O2 interaction.

Botrytis↗
PubMed2006

Oscillatory reactions involving hydrogen peroxide and thiosulfate-kinetics of the oxidation of tetrathionate by hydrogen peroxide.

The reaction between tetrathionate and hydrogen peroxide forms an important part of several pH oscillators based on the oxidation of thiosulfate. The kinetics of this reaction were examined in a batch reactor by measurement of the initial pH values in the range from 8 to 10.5. Experimental data were evaluated by the method of initial reaction rates combined with the assumption of instantaneously equilibrated acid-base reactions. The rate-determining step was found to be of the first order with respect to tetrathionate, hydrogen peroxide, and OH- ions with the value of rate constant k = (1.50 +/- 0.03) x 10(2) (M2 s)(-1) at 25 degrees C. In the alkaline solution, no distinct catalytic effect of Cu2+ was observed in contrast to earlier assumptions. The waveform of measured pH over the course of the reaction indicates that thiosulfate is probably an intermediate because characteristics of the curves are very similar to those for the oxidation of thiosulfate. We also measured the time evolution of concentrations of major components by the attenuated total internal reflectance infrared spectroscopy to further elucidate the underlying reaction mechanism. These measurements confirm the suspected role of thiosulfate as an intermediate in the studied reaction and provide valuable detailed information on the time evolution of thiosulfate, sulfite, sulfate, tetrathionate, and trithionate. These experimental observations are included in a simple mechanism that accurately simulates the reaction course in an alkaline solution. The results provide considerable new insights into the nature of autocatalysis in the hydrogen peroxide-thiosulfate-Cu2+ reaction and suggest that a new role for Cu2+ in the oscillatory dynamics observed in a flow-through reactor needs to be found.

Hydrogen Peroxide↗
PubMed1985

Increased release of hydrogen peroxide and superoxide anion from asbestos-primed macrophages. Effect of hydrogen peroxide on the functional activity of alpha 1-protease inhibitor.

The ability of asbestos-elicited murine peritoneal macrophages to release superoxide anion and hydrogen peroxide, following in vitro triggering, has been investigated. The asbestos-elicited macrophages produced increased levels of superoxide and hydrogen peroxide compared to control macrophages and similar levels to those produced by Corynebacterium parvum elicited macrophages. The supernatants from asbestos-elicited macrophages which had been triggered in vitro were capable of impairing the ability of alpha 1-protease inhibitor to inhibit elastase function. The catalase sensitivity of this effect showed it to be due to hydrogen peroxide.

Animals↗
PubMed2006

Distillation kinetics of solid mixtures of hydrogen peroxide and water and the isolation of pure hydrogen peroxide in ultrahigh vacuum.

We present results of the growth of thin films of crystalline H2O2 and H2O2*2H2O (dihydrate) in ultrahigh vacuum by distilling an aqueous solution of hydrogen peroxide. We traced the process using infrared reflectance spectroscopy, mass loss on a quartz crystal microbalance, and in a few cases ultraviolet-visible reflectance. We find that the different crystalline phases-water, dihydrate, and hydrogen peroxide-have very different sublimation rates, making distillation efficient to isolate the less volatile component, crystalline H2O2.

Journal Article↗
PubMed2003

Activation of hydrogen peroxide through hydrogen-bonding interaction with acidic alcohols: epoxidation of alkenes in phenol.

[reaction: see text] Electrophilic activation of hydrogen peroxide can be achieved in acidic alcohol solvents without the need for a metal catalyst. This concept is illustrated by the epoxidation of alkenes with H(2)O(2) employing phenol as a solvent. It is proposed that intermolecular hydrogen bonding between H(2)O(2) and phenol activates H(2)O(2) for oxygen-atom transfer. In this interaction, the role of phenol is purely catalytic.

Journal Article↗
PubMed2002

Exhaled hydrogen peroxide, nitrite and nitric oxide in healthy children: decrease of hydrogen peroxide by atmospheric nitric oxide.

Hydrogen peroxide (H2O2) and nitrite (NO2-) in exhaled breath condensate have recently been suggested as non-invasive markers of airway inflammation. The goal of this study was to clarify the role of factors that may potentially influence the measurement of H2O2 and nitrite and to look for possible correlations among these inflammatory markers. H2O2 and nitrite values were assessed fluorometrically in breath condensate of 102 healthy children (age 4-18 years) and a detailed status of atopy (including history, lung function and skin prick test) was taken in all children. To find out the role of atmospheric nitric oxide, eNO and envNO were measured via chemiluminescence in association with the sampling of the breath condensate. Median (interquartile range) H2O2 was 0.51 (0.26 - 0.74) microM and nitrite was 3.3 (2.7 4.1) microM. A significant negative correlation between H2O2 and envNO was observed (r = -0.50; p < 0.0001). ENO was independent of envNO at our envNO range up to 56 ppb. No further correlation was found. The inflammatory markers in exhaled breath condensate H2O2, nitrite and eNO are not interrelated to each other in healthy children. Whereas eNO was not dependent on envNO values, high envNO values must be taken into account when measuring H2O2 in exhaled breath condensate.

Adolescent↗
PubMed1997

The importance of sodium pyruvate in assessing damage produced by hydrogen peroxide.

Instability of hydrogen peroxide solutions was noted during the experimental exposure of human cells in culture to hydrogen peroxide in experiments designed to study the production and repair of DNA single-strand breaks. A hydrogen peroxide concentrate was diluted into culture medium, which was then added to experimental cell cultures at various times, with all cultures assessed for DNA damage at 2 h. Only cells treated by the first addition had observable DNA damage. This result was unexpected since these cells had had the maximum repair time. It was determined that the hydrogen peroxide had been eliminated by the culture medium. To determine the mechanism of this elimination, 200 microM hydrogen peroxide was added to various cell culture components, and the solutions were assayed for hydrogen peroxide after 1 h at 37 degrees C. Although most components (except the balanced salts) showed some hydrogen peroxide degradation, it was found that sodium pyruvate was most effective, by a wide margin, in eliminating hydrogen peroxide and its toxic effects. This was confirmed by addition of pyruvate to balanced salt solutions or buffers, and observing the same elimination of hydrogen peroxide. We subsequently found a few earlier reports describing the decarboxylation reaction between hydrogen peroxide and pyruvate, but no kinetic measurements have been published and there seems to be no general appreciation for the very high efficiency of this reaction. The present work presents a preliminary assessment of the importance of pyruvate in the study of hydrogen peroxide and other reactive oxygen species in mammalian cell culture.

Azides↗
PubMed2006

Nitric oxide increases toxicity of hydrogen peroxide against rat liver endothelial cells and hepatocytes by inhibition of hydrogen peroxide degradation.

Nitric oxide (NO) and hydrogen peroxide (H(2)O(2)) show cooperativity in their cytotoxic action. The present study was performed to decipher the mechanisms underlying this phenomenon. In cultured liver endothelial cells and in cultured, glutathione-depleted hepatocytes, the combined exposure to NO (released by spermine NONOate, 1 mM) and H(2)O(2) (released by glucose oxidase) induced cell injury that was far higher than the injury elicited by NO or H(2)O(2) alone. In both cell types, the addition of the NO donor increased H(2)O(2) steady-state levels, although with different kinetics: in hepatocytes, the increase in H(2)O(2) levels was already evident at early time points while in liver endothelial cells it became evident after > or =2 h of incubation. NO exposure inhibited H(2)O(2) degradation, assessed after addition of 50 microM, 200 microM, or 4 mM authentic H(2)O(2), significantly in both cell types. However, again, early and delayed inhibition was observed. The late inhibition of H(2)O(2) degradation in endothelial cells was paralleled by a decrease in glutathione peroxidase activity. Glutathione peroxidase inactivation was prevented by hypoxia or by ascorbate, suggesting inactivation by reactive nitrogen oxide species (NO(x)). Early inhibition of H(2)O(2) degradation by NO, in contrast, could be mimicked by the catalase inhibitor azide. Together, these results suggest that the cooperative effect of NO and H(2)O(2) is due to inhibition of H(2)O(2) degradation by NO, namely to inhibition of catalase by NO itself (predominant in hepatocytes) and/or to inhibition of glutathione peroxidase by NO(x) (prevailing in endothelial cells).

Animals↗
PubMed1989

Effect of pH on the spectrum of cytochrome c oxidase hydrogen peroxide complex.

Hydrogen peroxide binding to ferric cytochrome c oxidase in proteoliposomes brings about a red-shift of the enzyme Soret band and increased absorption in the visible range with two prominent peaks at approx. 570 and 607 nm. The molar absorptivity of the H2O2-induced difference spectrum is virtually pH-independent in the Soret band and at 570 nm, whereas the peak at 607 nm increases approx. 3-fold upon alkalinization in a narrow pH range 6.0-7.2, the effect being reversible. The pH profile of this transition indicates ionization of two acid-base groups with close pK values of 6.7. The lineshape of the peroxide compound difference spectrum is found to respond to pH changes inside the proteoliposomes. It is suggested that peroxide-complexed enzyme can undergo a pH-dependent transition to a form with increased extinction at 605-607 nm, possibly corresponding to the 420 nm (or 'pulsed') conformer of the ferric cytochrome oxidase formed as an early product of the enzyme oxidation. Accordingly, relaxation of the '420 nm' form to the resting state would be linked to an uptake of two protons from the M-aqueous phase. This protolytic reaction might be a partial step of the cytochrome oxidase proton pumping mechanism or it could serve to regulate interconversion between the active 'pulsed' and less active 'resting' states of the enzyme in the membrane.

Animals↗
PubMed1987

Hydrogen peroxide or heat shock induces resistance to hydrogen peroxide in Chinese hamster fibroblasts.

Survival after H2O2 exposure or heat shock of asynchronous Chinese hamster ovary cells (HA-1) was assayed following pretreatment with mildly toxic doses of either H2O2 or hyperthermia. H2O2 cytotoxicity at 37 degrees C, expressed as a function of mM H2O2 was found to be dependent on cell density at the time of treatment. The density dependence reflected the ability of cells to reduce the effectiveness of H2O2 as a cytotoxic agent. When the survival data were plotted as a function of mumoles H2O2/cell at the beginning of the treatment, survival was independent of cell density. Cells pretreated with 0.1 mM (3-5 mumoles/cell X 10(-7)) H2O2 for 1 hr at 37 degrees C (30-50% survival) became resistant to a subsequent H2O2 treatment 16-36 hr after pretreatment [dose modifying factor (DMF) at 1% isosurvival = 4-6]. Their resistance to 43 degrees C heating, however, was only slightly increased over controls 16-36 hr following pretreatment (DMF at 1% isosurvival = 1.2). During this same interval, the synthesis of protein migrating in the 70 kD region of a one-dimensional SDS-polyacrylamide gel was enhanced twofold in the H2O2-pretreated cells. When the cells were heated for 15 min at 45 degrees C (40-60% survival), the survivors became extremely resistant to 43 degrees C heating and somewhat resistant to H2O2 (DMF at 1% isosurvival = 2). The heat-induced resistance to heat developed much more rapidly (reached a maximum between 6 and 13 hr) following pretreatment than the heat-induced resistance to H2O2 (16-36 hr). The enhanced synthesis of 70 kD protein after heat shock was greater in magnitude and occurred more rapidly following preheating than following H2O2 pretreatment. The cells that became resistant to H2O2 by either pretreatment (H2O2 or heat shock) also increased their ability to reduce the H2O2 cytotoxicity from the treatment medium beyond that of the untreated HA-1 cells. This may be one of the mechanisms involved in the increased resistance and a common adaptive mechanism induced by both stresses. These data indicate that mammalian cells develop resistance to H2O2 following mild pretreatment with H2O2 or heat shock. The cross-resistance induced by H2O2 and heat shock reinforce the hypothesis that some overlap in mechanisms exist between the cellular responses to these two stresses. However, the failure of H2O2 pretreatment to induce much resistance to heat indicates that there are also differences in the actions of the two agents.

Animals↗
PubMed1988

The interaction of oxymyoglobin with hydrogen peroxide: a kinetic anomaly at large excesses of hydrogen peroxide.

The reaction of oxymyoglobin (MbO2) with H2O2 has been examined at pH 7.2 and 20(+/- 2) degrees C for reactant ratios of [H2O2]:[MbO2] greater than approximately 15:1. Under the conditions of large excesses of H2O2, the reaction is characterized by an increase in the rate of loss of MbO2 as [H2O2] is increased, for which a value of k(MbO2 + H2O2) approximately 3 M-1 s-1 is obtained. This kinetic behavior contrasts the saturation kinetics observed previously at lower values of [H2O2]. The change in kinetics at increasing excesses of H2O2 is accompanied by a progressive tendency toward the direct formation of ferrimyoglobin at the expense of ferrylmyoglobin formation. A mechanism is proposed in which an initially formed intermediate produces the ferryl derivative in competition with the formation of ferrimyoglobin through the interaction of further H2O2. Overall, the H2O2 is catalytically decomposed by the MbO2. This mechanism is integrated with that determined previously at low excesses of H2O2 into a complex general scheme that applies over the entire studied range of [H2O2]:[MbO2]. No evidence is obtained for the conversion of ferrylmyoglobin to oxymyoglobin by the large excesses of H2O2, regardless of whether the ferryl derivative is the product of the reaction of H2O2 with the oxy or ferri derivative of myoglobin.

Chemical Phenomena↗
PubMed1993

[The causes of death in animals with hydrogen peroxide poisoning].

Hydrogen peroxide (HP) was administered to experimental rats at the level of LD100. The indices of external breathing, blood pressure, ECG, heart thrust were determined. It was found that the increasing tonus of the vagus nucleus was an essential feature of the pathogenesis of HP poisoning, inducing a series of pathological changes in animals. A certain role was played by extensive gas embolism. About 80% of the experimental animals survived after administration of atropine or lobeline.

Acute Disease↗
PubMed2005

AtGLB1 enhances the tolerance of Arabidopsis to hydrogen peroxide stress.

Hydrogen peroxide (H2O2) as a widespread molecule plays an important role in plant stress responses. Here, we showed that an Arabidopsis line overexpressing hemoglobin 1 (AtGLB1) can enhance its tolerance to severe hypoxic stress. In our research, Arabidopsis lines with different hemoglobin levels were employed to study the relationship between H2O2 level and the tolerance to hypoxic stress. The relatively low endogenous H2O2 level of AtGLB1-overexpressing plants could be one of the main factors for the increased tolerance of plants to hypoxic stress. Further investigation indicated that the activity of the antioxidant system involved in scavenging H2O2 increased in all three lines examined during hypoxic treatment, while only the line overexpressing AtGLB1 could retain these relatively high levels up to 48 h of the treatment, suggesting that the antioxidant system might play a role in the low H2O2 level of Arabidopsis overexpressing AtGLB1.

Adaptation, Physiological↗
PubMed1989

Relationship between changes in ploidy and stable cellular resistance to hydrogen peroxide.

Stable hydrogen peroxide (H2O2)-resistant variants of the Chinese hamster ovary HA-1 line have been isolated by culturing cells in progressively increasing concentrations of H2O2 (greater than 200 days, in 50-800 microM H2O2). Increases in catalase activity in these variant cell lines were shown to correlate with increased H2O2 resistance. Stable (greater than 240 days) H2O2-resistant cell lines, seven quasidiploid (21-22 chromosomes/cell) and six quasitetraploid (40-44 chromosomes/cell) were clonally isolated from the 800 microM adapted H2O2-resistant variants which were heterogeneous with respect to ploidy. The H2O2 dose-modifying factors (DMFs) were 3, 5, 8, 13, 15, 26, and 27 for the seven quasidiploid cell lines, and 21, 32, 38, 40, 42, and 49 for the six quasitetraploid cell lines. The mean DMF was 14 +/- 10 for the former and 37 +/- 10 for the latter. Our data show that on the average the quasitetraploid cell lines were significantly more resistant to H2O2-mediated cell killing than the quasidiploid cell lines derived from the same mixed population of 800 microM H2O2-adapted cells. When catalase activities (k units/cell) of the HA-1 cells and three of the clonally derived cell lines (two quasidiploid and one quasitetraploid) were determined and plotted vs. H2O2-DMF, a positive linear correlation was obtained (correlation coefficient = 0.99). This result was further confirmed when immunoreactive catalase protein/cell was detected by Western blots. Our data show that chronic exposure of cells to H2O2 stress (800 microM) was accompanied by increases in quasitetraploid cells within the population. Quasitetraploid cell lines derived from this population demonstrated increased stable H2O2-resistance which may be related to stable increases in the expression of catalase.

Animals↗
PubMed1985

A study of the sensitivity of Leishmania donovani promastigotes and amastigotes to hydrogen peroxide. I. Differences in sensitivity correlate with parasite-mediated removal of hydrogen peroxide.

The sensitivities of promastigotes and amastigotes of Leishmania donovani to reagent or glucose oxidase-generated hydrogen peroxide (H2O2) were examined in a phagocyte-free system and compared with direct measurements of loss of H2O2 due to reaction with the parasite. Using a combined fluorescence dye uptake/dye exclusion viability assay in conjunction with motility and transformation data it was shown that log-phase promastigotes harvested from recently transformed cultures were intermediate in their H2O2 sensitivity between amastigotes and log-phase promastigotes harvested from long-term subcultures. It was also observed that, while promastigotes are equally sensitive to either form of H2O2 stress, amastigotes are more resistant to single larger amounts of reagent H2O2 than to equivalent amounts of H2O2 generated over a 1 h period. In each case the respective LD50 values obtained for each form of the parasite under each type of H2O2 stress correlated with saturation of their ability to remove H2O2 from the phagocyte-free system. For both promastigotes and amastigotes there was always a time delay after removal of either form of H2O2 stress before H2O2-mediated damage to membranes became apparent. The results suggest that the differential responses of promastigotes and amastigotes to different forms of H2O2 stress may depend upon different H2O2 scavenging mechanisms examined in more detail in the accompanying paper.

Animals↗