Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “OXIDATION REDUCTION”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,585 records · Page 88Linked to original sources

Oxidation and reduction of sulfite by chloroplasts and formation of sulfite addition compounds.

After exposing intact chloroplasts isolated from spinach (Spinacia oleracea L. cv Yates) and capable of photoreducing CO(2) at high rates to different concentrations of radioactive sulfite in the light or in the dark, (35)SO(2) and H(2) (35)S were removed from the acidified suspensions in a stream of nitrogen. Remaining activity could be fractionated into sulfate, organic sulfides, and sulfite addition compounds. When chloroplast suspensions contained catalase, superoxide dismutase and O-acetylserine, the oxidation of sulfite to sulfate was slower in the light than the reductive formation of sulfides that exhibited a maximum rate of about 2 micromoles per milligram chlorophyll per hour, equivalent to about 1% of maximum carbon assimilation. Botht the oxidative and the reductive detoxification of sulfite were very slow in the dark. Oxidation was somewhat, but not much, accelerated in the light in the absence of O-acetylserine, which caused a dramatic decrease in the formation of organic sulfides and an equally dramatic increase in the concentration of sulfite addition compounds whose formation was light-dependent. The sulfite addition compounds were not identified. Addition compounds did not accumulate in the dark. In the light, the electron transport inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethylurea, diuron, decreased not only the reduction, but also the oxidation of sulfite and the formation of addition compounds.

Journal Article↗

Paraquat toxicity and oxidative damage. Reduction by melatonin.

The ability of melatonin to protect against paraquat-induced oxidative damage in rat lung, liver, and serum was examined. Changes in the levels of malondialdehyde (MDA) plus 4-hydroxyalkenals (4-HDA) and reduced and oxidized glutathione concentrations were measured. Paraquat (50 mg/kg) was injected i.p. into either Sprague-Dawley or Wistar rats with or without the co-administration of 5 mg/kg melatonin. Paraquat alone increased MDA + 4-HDA levels in serum and lungs of both rat strains, with these increases being abolished by melatonin co-treatment. Paraquat also decreased reduced glutathione levels and increased oxidized glutathione concentrations in lung and liver; these changes were negated by melatonin. The effect of melatonin on paraquat-induced mortality was also studied. Paraquat at a dose of 79 mg/kg was lethal for 50% of animals within 24 hr; when administered together with melatonin, the LD50 for paraquat increased to 251 mg/kg.

Animals↗

Redox- and oxidant-mediated regulation of interleukin-10: an anti-inflammatory, antioxidant cytokine?

Reduction-oxidation (redox) state constitutes such a potential signaling mechanism for the regulation of an inflammatory signal associated with oxidative stress. Interleukin (IL)-10 has recently emerged as an anti-inflammatory cytokine with antioxidant properties. Interestingly, redox- and oxidant-mediated pathways positively and/or negatively regulate the expression, distribution, and functional properties of IL-10, thus, allowing the evolution of what is known as an anti-inflammatory redox-oxidant revolving axis. This axis is directly involved in regulating phosphorylation mechanisms, which eventually control gene expression and the biosynthesis of oxidative stress-related cofactors, such as reactive species and inflammatory cytokines. The association between IL-10, an anti-inflammatory antioxidant, with redox- and oxidant-related pathways governing the regulation of inflammatory and closely dependent processes is thereafter discussed.

Animals↗

Thermodynamic and kinetic considerations of Q-cycle mechanisms and the oxidant-induced reduction of cytochromes b.

In coenzyme Q-cycles, it is proposed that one electron from the quinol reduces the Rieske iron sulfur center (Em approximately 280 mV) and the remaining electron on the semiquinone reduces cytochrome br (Em approximately -60 mV). The Em for the two-electron oxidation of the quinol is approximately 60 mV and therefore the reduction of cytochrome bT by quinol is not favorable. As the stability constant for the dismutation of the semiquinone decreases, the calculated Em for the Q/QH. couple is lowered to values below the Em of cytochrome bT. Contemporary coenzyme Q-cycles are based on the belief that the lower value for the Em of the Q/QH. couple compared to the Em for cytochrome bT means that the semiquinone is a spontaneous reducing agent for the b-cytochrome. The analysis in the paper shows that this is not necessarily so and that neither binding sites nor ionization of the semiquinone per se alters this situation. For a Q-cycle mechanism to function, ad hoc provisions must be made to drive the otherwise unfavorable reduction of cytochrome bT by the semiquinone or for the simultaneous transfer of both electrons to cytochrome bT and cytochrome c1 (or the iron sulfur protein). Q-cycle mechanisms with these additional provisions can explain the observation thus far accumulated. A linear path which is functionally altered by conformational changes may also explain the data.

Cytochrome b Group↗

Oxidation and reduction of nitrite ion in the TiO2 photo-induced catalytic reaction.

During a photo-induced catalytic reaction under near UV irradiation to an aqueous suspension of Ti4O2, about 95% of NO2- was oxidized to NO3-, but NH4+ was not detected. The oxidation was inhibited by the addition of mannitol or under anaerobic conditions. The nitration of HPA was observed in the presence of t-buthanol, suggesting the formation of ONOO. An ESR spectrum gave a triplet signal at g = 2.041,in the presence of NO2-, mannitol, FeSO4, and MGD, indicating the reduction of NO2- to NO.

Catalysis↗

Pigment production from tryptophan by an Achromobacter species.

Duerre, John A. (University of North Dakota, Grand Forks), and Patrick J. Buckley. Pigment production from tryptophan by an Achromobacter species. J. Bacteriol. 90:1686-1691. 1965.-A microorganism was isolated from the soil near the University of North Dakota. Biochemical and morphological characteristics indicated that this organism would best be classified as a member of the family Achromobacteraceae, genus Achromobacter, species unknown. The organism produced a red pigment when grown in a medium containing yeast extract and tryptophan. The pH optimum for pigment production was about 8.0 and the optimal temperature was 25 C. During a study of the nutritional requirements for growth and pigment production, it was found that the organism would grow and produce pigment in a medium containing tryptophan and nucleosides, but the rate of both growth and pigment formation in this medium was slower than that observed with tryptophan and yeast extract. The organism grew well in the presence of acid-hydrolyzed casein and nucleosides without producing pigment, indicating that the pigment is not necessary for growth. Resting-cell experiments definitely established tryptophan as the sole exogenous requirement for pigment production. The pigment was extracted from yeast extract-tryptophan medium with chloroform. Thin layer chromatographic analysis of the crude pigment extracted from this medium revealed the presence of two other pigments in addition to the major red pigment. One of these was a highly fluorescent orange pigment and the other a pink pigment. Only the red pigment was produced by resting cells in the presence of tryptophan alone. This pigment served as an electron acceptor when coupled with formic dehydrogenase, indicating its possible function as an oxidation-reduction pigment. The oxidized pigment had absorption peaks at 506 and 304 mmu. The peak at 506 mmu disappeared upon reduction with sodium sulfite. Shaking the reduced pigment in air proved to be an unsatisfactory method for returning the reduced pigment to the oxidized, colored state.

Alcaligenes↗

Gamma interferon production by hepatic NK T cells during Escherichia coli infection is resistant to the inhibitory effects of oxidative stress.

The reductive-oxidative status of tissues regulates the expression of many inflammatory genes that are induced during gram-negative bacterial infections. The cytokine gamma interferon (IFN-gamma) is a potent stimulus for host inflammatory gene expression, and oxidative stress has been shown to inhibit its production in mice challenged with Escherichia coli bacteria. The objective of the present study was to characterize the cells that produced IFN-gamma in a mouse bacterial peritonitis model and determine the effects of oxidative stress on their activation. The liver contained large numbers of IFN-gamma-expressing lymphocytes following challenge with viable E. coli bacteria. The surface phenotypes of IFN-gamma-expressing hepatic lymphocytes were those of natural killer (NK) cells (NK1.1(+) CD3(-)), conventional T cells (NK1.1(-) CD3(+)), and NK T cells (NK1.1(+) CD3(+)). Treating mice with diethyl maleate to deplete tissue thiols significantly impaired IFN-gamma production by NK cells, conventional T cells, and CD1d-restricted NK T cells in response to E. coli challenge. However, IFN-gamma expression by a subset of NK T cells, which did not bind alpha-galactosylceramide-CD1d tetramers, was resistant to the inhibitory effects of tissue oxidative stress. Stress-resistant IFN-gamma-expressing cells were also predominantly CD8(+) and bore gamma delta T-cell antigen receptors. The residual IFN-gamma response by NK T cells may explain previous reports of hepatic gene expression following gram-negative bacterial challenge in thiol-depleted mice. The finding also demonstrates that innate immune cells differ significantly in their responses to altered tissue redox status.

Animals↗

One-electron oxidation and reduction reactions of vitamin C derivatives: 6-bromo- and 6-chloro-6-deoxy-ascorbic acid.

6-Bromo- and 6-chloro-6-deoxy derivatives of ascorbate anion are able to transfer an electron to the oxidizing radicals .OH, Br2.- and RS. with the same rate constants as the ascorbate anion itself. The resulting radicals also show the same kinetic stabilities and optical absorption spectra as the well-characterized ascorbate radical anion (lambda max = 360 nm; epsilon 360 = 330 m2 mol-1). This proves that there is no influence of the structural changes in the side chain on the antioxidant capacity of the ascorbate moiety. In contrast, measured reduction of the 6-halo-6-deoxy derivatives occurs significantly faster (up to one order of magnitude) than the reduction of unsubstituted ascorbate. For example, absolute rate constants of 4.6 x 10(9) and 2.2 x 10(7) dm3 mol-1 s-1 have been measured for the reactions of bromo-derivative with eaq- and (CH3)2COH respectively. These radical-induced reductions proceed via dissociative electron capture and, under cleavage of the C-halogen bond, yield C-6 carbon-centered radicals. In the presence of oxygen the corresponding peroxyl radical is readily formed. This radical is again able to oxidize the ascorbate moiety (rate constant 2 x 10(7) dm3 mol-1 s-1). Results are discussed in terms of biological relevance of the investigated compounds regarding their ability to act as efficient antioxidants and bioreductive antitumour agents simultaneously.

Ascorbic Acid↗

Genetic characterization of a single bifunctional enzyme for fumarate reduction and succinate oxidation in Geobacter sulfurreducens and engineering of fumarate reduction in Geobacter metallireducens.

The mechanism of fumarate reduction in Geobacter sulfurreducens was investigated. The genome contained genes encoding a heterotrimeric fumarate reductase, FrdCAB, with homology to the fumarate reductase of Wolinella succinogenes and the succinate dehydrogenase of Bacillus subtilis. Mutation of the putative catalytic subunit of the enzyme resulted in a strain that lacked fumarate reductase activity and was unable to grow with fumarate as the terminal electron acceptor. The mutant strain also lacked succinate dehydrogenase activity and did not grow with acetate as the electron donor and Fe(III) as the electron acceptor. The mutant strain could grow with acetate as the electron donor and Fe(III) as the electron acceptor if fumarate was provided to alleviate the need for succinate dehydrogenase activity in the tricarboxylic acid cycle. The growth rate of the mutant strain under these conditions was faster and the cell yields were higher than for wild type grown under conditions requiring succinate dehydrogenase activity, suggesting that the succinate dehydrogenase reaction consumes energy. An orthologous frdCAB operon was present in Geobacter metallireducens, which cannot grow with fumarate as the terminal electron acceptor. When a putative dicarboxylic acid transporter from G. sulfurreducens was expressed in G. metallireducens, growth with fumarate as the sole electron acceptor was possible. These results demonstrate that, unlike previously described organisms, G. sulfurreducens and possibly G. metallireducens use the same enzyme for both fumarate reduction and succinate oxidation in vivo.

Culture Media↗

Interactive control of Rhodobacter capsulatus redox-balancing systems during phototrophic metabolism.

In nonsulfur purple bacteria, redox homeostasis is achieved by the coordinate control of various oxidation-reduction balancing mechanisms during phototrophic anaerobic respiration. In this study, the ability of Rhodobacter capsulatus to maintain a balanced intracellular oxidation-reduction potential was considered; in addition, interrelationships between the control of known redox-balancing systems, the Calvin-Benson-Bassham, dinitrogenase and dimethyl sulfoxide reductase systems, were probed in strains grown under both photoheterotrophic and photoautotrophic growth conditions. By using cbb(I) (cbb form I operon)-, cbb(II)-, nifH-, and dorC-reporter gene fusions, it was demonstrated that each redox-balancing system responds to specific metabolic circumstances under phototrophic growth conditions. In specific mutant strains of R. capsulatus, expression of both the Calvin-Benson-Bassham and dinitrogenase systems was influenced by dimethyl sulfoxide respiration. Under photoheterotrophic growth conditions, coordinate control of redox-balancing systems was further manifested in ribulose 1,5-bisphosphate carboxylase/oxygenase and phosphoribulokinase deletion strains. These findings demonstrated the existence of interactive control mechanisms that govern the diverse means by which R. capsulatus maintains redox poise during photoheterotrophic and photoautotrophic growth.

Bacterial Proteins↗

Role of protein disulfide isomerase in molecular fate of thyroglobulin and its regulation by endogenous oxidants and reductants.

The molecular fate of thyroglobulin (Tg) is controlled by oligomerization, a means of storing Tg at high concentrations, and deoligomerization. The oligomerization of bovine Tg are intermolecular reactions that occur through oxidative processes, such as disulfide and dityrosine formation, as well as isopeptide formation; disulfide formation is primarily responsible for Tg oligomerization. Here, the protein disulfide isomerase (PDI) and/or peroxidase-induced oligomerization of unfolded thyroglobulins, which were prepared by treating bovine Tg with heat, urea or thiol/urea, was investigated using SDS-PAGE analyses. In addition, the enzymatic oligomerization was compared with non-enzymatic oligomerization. The thermally-induced oilgomerization of Tg, dependent on glutathione redox state, was affected by the ionic strength or the presence of a surfactant. Meanwhile, PDI-catalyzed oligomerization, time and pH-dependent, was the most remarkable with unfolded/reduced Tg, which was prepared from a treatment with urea/DTT, while the thermally-unfolded Tg was less sensitive. Similarly, the oligomerization of unfolded/reduced Tg was also mediated by peroxidase. However, PDI showed no remarkable effect on the peroxidase-mediated oligomerization of either the unfolded or unfolded/reduced Tg. Additionally, the reductive deoligomerization of oligomeric Tg was exerted by PDI in an excessively reducing state. Based on these results, it is proposed that PDI catalyzes the oligomerization of Tg through the disulfide linkage and its deoligomerization in the molecular fate, and this process may require a specific molecular form of Tg, optimally unfolded/reduced, in a proper redox state.

Animals↗

Effects of sensitizers on cell respiration: 1. Factors influencing the effects of hypoxic cell radiosensitizers on oxygen utilization of tumour and cultured mammalian cells.

We have investigated the effects of 24 nitrocompounds, differing in their half-reduction potential, on the respiration in vitro of Ehrlich ascites tumour cells and cultured V79 lung cells. Many drugs with redox potentials more positive than--0.35 stimulated oxygen utilization in the presence of glucose. Glucose had little effect on the inhibition of respiration by drugs with oxidation-reduction potentials more negative than--0.38. Nitrocompounds that inhibited Ehrilch cell respiration in the presence of glucose, also inhibited intracellular reduction of ferricytochrome (c+c1). Drugs that stimulated oxygen utilization also stimuated intracellular (c " c1). Drugs that stimulated oxygen utilization also stimulated intracellular reduction of ferricytochrome (c + c1). A correlation between drug oxidation-reduction potential and stimulation of oxygen utilization in KCN-inhibited cells was found.

Animals↗

Diverse NO reduction by Halomonas halodenitrificans nitric oxide reductase.

Reduction of the four Fe centers is not required to initiate the reaction of the Halomonas halodenitrificans nitric oxide reductase (NOR) based on the facts that NOR in the form that ferric heme b(3) and non-heme iron (Fe(B)) are not bridged and/or the interaction between them is weakened and reversibly binds NO molecules, and that NOR in the form that only heme b(3) is oxidized reacts with NO molecules.

Enzyme Activation↗

The formation of 1-hydroxymethylnaphthalene and 6-hydroxymethylquinoline by both oxidative and reductive routes in Cunninghamella elegans.

Extraction of medium after incubation of the fungus, Cunninghamella elegans, with 0.03% (w/v) 1-methylnaphthalene produced mainly 1-hydroxymethylnaphthalene together with some 1-naphthoic acid and hydroxynaphthoic acid. Higher concentrations of substrate were inhibitory to biotransformation. Similar incubations with 1-naphtoic acid as substrate resulted in reduction of the carboxyl group to give 1-hydroxymethylnaphthalene. When 6-methylquinoline was used, the main product was 6-hydroxymethylquinoline but also some quinoline-6-carboxylic acid and some 6-methylquinoline-N-oxide were identified. In a 2-l fermenter 2.5 g substrate was transformed in 324 h. The 6-hydroxymethylquinoline was also produced by reduction of quinoline-6-carboxylic acid by the organism.

Biodegradation, Environmental↗

Role of nitrite and nitrate as a redox couple in the rat colon. Implications for diarrheal conditions.

Colonic levels of nitrite and circulating levels of nitrate are elevated in subjects with chronic diarrhea. The role of colonic epithelial cells in oxidation-reduction of nitrite and consequent control of nitrite and nitrate levels is unknown. Isolated rat colonocytes and isolated loops of colon were used to study oxidation and reduction of nitrate and nitrite. Colonocytes oxidized nitrite to nitrate at a rate of 162 +/- 33 nmol/min.g (dry wt) (n = 6) over 0-20 min, a value increased by addition of 5 mM glucose and 1 mM nicotinamide adenine dinucleotide (p = less than 0.01), but not altered by antibiotics. Nitrite oxidation correlated linearly with the dry weight of isolated colonocytes (r = 0.92), indicating a cellular reaction. Nitrite was absorbed at a rate of 0.28 nmol/min.cm2 (n = 9) from the colonic lumen, which reflected 74% absorption of the available nitrite. Of the absorbed nitrite, 14.3% reappeared in the colonic lumen as nitrate. Colonocytes may be important in oxidizing nitrite to nitrate, thus preventing excess nitrite from entering into the circulation and returning some nitrate to the colonic lumen for respiration by anaerobic bacteria. The interaction of nitrites and colonocytes deserves further study with regard to the oxidation-reduction of nitrite and to the development of colonic neoplasia in chronic diarrheal conditions.

Animals↗

[Protective effect of antioxidants in methemoglobinemia caused by sodium nitrite in experimental studies].

Sodium nitrite induced poisoning resulted into oxidation-reduction disorders with concomitant changes in the ratio of the oxidated and reduced forms towards accumulation of the oxidated equivalents. Antioxidants unithiol, tocopherol acetate, ascorbic acid, methylene blue, violuric acid influenced the oxidation-reduction balance in different ways. The protective action of violuric acid was comparable with that of methylene blue and exceeded the unithiol protective properties. Violuric acid, as compared with unithiol, ascorbic acid and tocopherol, was more effective in decreasing methemoglobin and nitrates contents in blood in methemoglobinemia cases. The violuric acid and methylene blue protective mechanisms are in all probability influenced by the antioxidant properties of these substances and their reductase activity.

Animals↗

Premature Salmonella Typhimurium growth inhibition in competition with other Gram-negative organisms is redox potential regulated via RpoS induction.

AIMS: To identify the role of oxidation-reduction (redox) potential in the premature growth inhibition and RpoS induction in Salmonella serotype Typhimurium in competitive growth experiments. METHODS AND RESULTS: Oxidation-reduction potential was measured throughout the growth of a minority population of Salm. Typhimurium in mixed cultures with other Gram-negative and Gram-positive organisms. A lux-based reporter was also used to evaluate RpoS activity in Salm. Typhimurium in competitor studies. In a mixed culture, the multiplication of a minority population of Salm. Typhimurium was inhibited when competing Gram-negative organisms entered the stationary phase. This was not seen when the competing flora was Gram-positive. The change in redox potential during growth in mixed cultures was closely linked to the inhibition of Salm. Typhimurium growth by Gram-negative competitors. An artificially induced drop in redox potential earlier during growth in mixed cultures with Gram-negative organisms reduced the time to RpoS induction in Salm. Typhimurium and thus inhibited its multiplication prematurely. In contrast, RpoS induction and growth inhibition were prevented under high redox potential conditions. CONCLUSIONS: This work shows that the inhibitory activity of competitive organisms can be mediated through their effect on redox potential-regulated RpoS induction. SIGNIFICANCE AND IMPACT OF THE STUDY: Redox potential is shown to be an important determinant of Salm. Typhimurium growth, an observation with practical implications both for its control and detection.

Antibiosis↗

Effect of potentiated solutions on mercury(II) signal in inversion voltammetry.

We studied the effects of homeopathically potentiated substances in ultralow doses on physicochemical properties of solutions. Inverse voltammetric signals during Hg(II) oxidation-reduction in the presence of potentiated water, lithium chloride, and mercury nitrate were studied by alternating-current inversion voltammetry. Potentiated substances modified oxidation-reduction processes in the electrochemical system. Potentiated solutions of Hg(II) increased the effective concentration (activity) of mercury ions. The effect was most significant in the presence of mercury nitrate in homeopathic dilutions C6+C12+C24. Our results indicate that potentiated substances specifically modulate kinetic and thermodynamic characteristics of solutions containing the same compounds.

Electrochemistry↗