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PubMed1999

The oxidation-reduction state of serum proteins in multiple sclerosis patients: effect of interferon beta-1b.

The concentration of reduction equivalents in serum was studied in a cohort of healthy individuals, in a group of multiple sclerosis (MS) patients undergoing treatment with interferon beta-1b and another group of MS patients who refused treatment with interferon beta-1b. Two classes of sulfhydryl groups were detectable in serum: (1) the uncovered sulfhydryls, accessible to the oxidation-reduction substrate 5,5-dithiobis-(-2-nitrobenzoic acid) (DTNB); and (2) the hidden sulfhydryls that required previous heat denaturation of serum proteins to become accessible to DTNB. The concentration of the reduced form of both the uncovered- and hidden-type of sulfhydryls was higher in the serum of MS patients than in healthy individuals. Interferon beta-1b lowered the plasma concentration of the uncovered reduced sulfhydryls after 3 months of treatment. This was in contrast to a minor effect of interferon beta-1b in the hidden-form of sulfhydryl groups. The results suggest that the concentration of reduced sulfhydryls is a biochemical marker of the in vivo oxidation/reduction reactions in MS.

Adult↗
PubMed1988

The oxidation-reduction kinetics of cytochromes b, c1 and c in initially fully reduced mitochondrial membranes are in agreement with the Q-cycle hypothesis.

Stopped-flow experiments were performed to distinguish between two hypotheses, the Q-cycle and the SQ-cycle, each describing the pathway of electron transfer in the QH2:cytochrome c oxidoreductases. It was observed that, when mitochondrial membranes from the yeast Saccharomyces cerevisiae were poised at a low redox potential with appropriate amounts of sodium dithionite to completely reduce cytochrome b, the kinetics of oxidation of cytochrome b showed a lag period of maximally 100 ms. Under the same experimental conditions, the oxidation-reduction kinetics of cytochromes c + c1 showed transient behaviour. These results do not support the presence of a mobile species of semiquinone in the QH2:cytochrome c oxidoreductases, as envisaged in the SQ-cycle, but are consistent with a Q-cycle mechanism in which the two quinone-binding domains do not exchange electrons directly on the timescale of turnover of the enzyme.

Antimycin A↗
PubMed2006

Mechanism of the oxidation-reduction of the MoVSbNbO catalyst: in operando X-ray absorption spectroscopy and electrical conductivity measurements.

The mechanism of the oxidation-reduction of the MoVSbNbO catalyst has been studied in dynamic conditions using X-ray absorption spectroscopy (XAS) and electrical conductivity measurements. XAS at Sb L1- and V/Mo K-edges permitted a better understanding of the chemical processes taking place in the M1 phase of the MoVSbNbO catalyst at different temperatures and atmosphere compositions. The reduction of antimony was already observed during the annealing of the M1 phase in He at 100 degrees C, which might be explained by the presence of hydrogen in the bronze-like structure of the M1 phase. Under operando conditions at 380 degrees C, we have found that Sb and V change their oxidation states depending on the C3H8/O2 ratio in the atmosphere. These changes occur simultaneously and with the same kinetics. Under the same conditions, variations in the oxidation state of Mo were not observed. These results prove that different types of oxygen (from the hexagonal channels and from the MO6 octahedral network) must be involved in the catalytic process although their relative contributions are different. It was found that the electrical conductance of the M1 phase correlates with the oxidation states of Sb and V and the concentration of oxygen vacancies.

Journal Article↗
PubMed1991

[Changes in neuronal structure and activity of various oxidation- reduction enzymes in the cerebellum after continuous long-term general low-frequency vibration].

In 84 white non-inbred rats, subjected to the effect of total continuous low-frequency vibration (8 Hz, 95 dB) for 1, 3, 7, 14, 20, 30 days, morphological and histoenzymatic changes have been studied in the nuclear neurons and in the cerebellar cortex. The former are presented as axonal reactions, as chromatolysis of various degree of manifestation, as changes in amount of hypochromic neurons, as glial reactions of various forms. They are interpreted as reactive and are of stage character. The histoenzymatic changes of the oxidation-reduction enzymes come to alterations in the activity of NAD and NADPH-dependent enzymes ratio and possible transformation of the cycle of tricarboxylic acids into the "incomplete" one. The structural and histoenzymatic changes correlate with each other.

Animals↗
PubMed1980

N-Oxide reduction by hemoglobin, cytochrome C and ferrous ions.

Indicine N-oxide is reduced to indicine by Fe(II) ions, by enzymatically reduced cytochrome c, and by ascorbic acid in conjunction with hemin or cytochrome c. Indicine N-oxide is not reduced by native hemoglobin, but is reduced by denatured hemoglobin. Oxygen competes with indicine N-oxide for reduction by denatured hemoglobin.

Antineoplastic Agents, Phytogenic↗
PubMed1990

Method for radio-capillary gas chromatography employing a modified oxidation-reduction train and flow-through detector.

A conventional radioactivity monitor was modified by reducing the volume of the oxidation-reduction train and gas proportional counting tube to permit coupled radio-capillary gas chromatographic analysis of labeled isomeric metabolites. The utility of this radioactivity monitoring technique was demonstrated by separating 3H-labeled sesquiterpene olefins. The advantages and limitations of mass (thermal conductivity) and radioactivity detection by this method are discussed.

Chromatography, Gas↗
PubMed1980

Energy status and oxidation-reduction status in rat liver at high altitude (3.8 km).

Adult male rats were exposed to 3.8-km altitude for intervals ranging from 1 h-60 d. Liver samples were taken under light ether anesthesia and were examined by enzymatic analyses. Within 1-6 h of hypoxic exposure, ATP levels decreased while ADP and AMP levels increased, producing a fall in calculated ATP/ADP and adenylate charge ratios. Concurrently, lactate/pyruvate and alpha-glycerophosphate/dihydroxyacetone phosphate ratios increased markedly. Direct measurements of cellular pyridine nucleotides indicated increased NADH/NAD and NADPH/NADP ratios. Levels of total adenosine phosphate and pyridine nucleotides decreased in a significant accompanying response. Many metabolite levels and calculated ratios returned to near-normal values within 1 week of exposure, indicating secondary intracellular adjustments to hypoxic stress; however, persistence of that stress is reflected in lactate conentrations and both substrate redox ratios. Results support and explore concepts that increased oxidation-reduction status and decreased energy status are primary events during hypoxia.

Adenine Nucleotides↗
PubMedDate not supplied

[Effect of corazole on the dynamics of oxidative-reductive processes in cerebral cortical neurons].

By using the complex of techniques on the basis of life-time microscopy and spectrophotometry of the structures of II, III layers of the cat brain motor cortex there was studied the effect of ionophoretically delivered corazole on the dynamics of integral redox-state of pyramidal cells bodies, the surrounding neuropil as compared to the changed bioelectrical activity. The development of the convulsant activity of neurons coincided with the shift of their redox-state towards the accumulation of intracellular reducing equivalents. Both in the bodies of neurons and in the structures of neuropil a stable pronounced increase of restoration of intracellular redox-systems was preceded by the process of wave-like fluctuating changes in the content of reducing equivalents. The role of the revealed disturbances of oxidation-reduction processes in the mechanisms of corazole-induced lesions of neurons is discussed.

Animals↗
PubMed1984

Role of the cellular oxidation-reduction state in methotrexate binding to dihydrofolate reductase and dissociation induced by reduced folates.

5-Formyltetrahydrofolate promotes the net dissociation of methotrexate bound to dihydrofolate reductase in the Ehrlich ascites tumor (L. H. Matherly et al., Cancer Res., 43: 2694-2699, 1983). Treatment of Ehrlich tumor cells with glucose or inhibitors of electron transfer stabilized the association of the antifolate with dihydrofolate reductase as reflected by a 2-fold increased fraction of dihydrofolate reductase-bound methotrexate and an abolition of the 5-formyltetrahydrofolate-induced dissociation of the inhibitor-enzyme complex. Glucose and azide were also found to increase the intracellular ratio of reduced nicotinamide adenine dinucleotide phosphate (NADPH) to oxidized nicotinamide adenine dinucleotide phosphate (NADP+) in the tumor approximately 8- and 11-fold, respectively. However, other agents which enhanced the association between methotrexate and its target enzyme were less effective in increasing the intracellular level of NADPH relative to NADP+. Micromolar concentrations of NADPH promoted methotrexate binding to the purified Ehrlich tumor dihydrofolate reductase. Bound methotrexate could be dissociated from the purified enzyme by 5-methyltetrahydrofolate but less readily by 5-formyltetrahydrofolate and only in the presence of reduced levels of NADPH relative to NADP+. The tetraglutamate derivative of 5-methyltetrahydrofolate was even more effective than the underivatized compound in dissociating methotrexate from dihydrofolate reductase. These findings suggest a critical role for the cellular oxidation-reduction state in determining the affinity of dihydrofolate reductase for methotrexate and thus the cellular sensitivity to the antifolate. In addition, the data are consistent with the possibility that dihydrofolate reductase is a key locus for intracellular competitive interactions between reduced folates and methotrexate during leucovorin rescue from the pharmacological effects of the antifolate.

Animals↗
PubMed1985

Improved myocardial preservation by control of the oxidation-reduction potential.

Simple cold storage remains the current method of preservation of human heart allografts between removal and transplantation, but this technique is not adequate for prolonged periods of preservation. An alternative to cold storage is machine perfusion of the isolated organ. Although this technique has yielded promising results in kidney preservation, there is limited experience with the heart. One factor limiting the effectiveness of perfusion preservation is the toxicity of oxygen free radicals generated during the perfusion. The generation and reduction of these radicals results in an electron transfer, producing an electrochemical potential known as the redox potential. This study examines the role of machine perfusion in heart preservation with and without the use of a new electrochemical cell that is able to control the redox potential during the perfusion. Hearts were preserved for twenty-four hours by either simple cold storage (Group I), or by machine perfusion with redox monitoring (Group II), or redox control (Group III). Control of the oxidation-reduction potential of the perfusate during machine perfusion of isolated hearts resulted in significantly improved systolic and diastolic function after perfusion compared to hearts that underwent machine perfusion without redox control or simple cold storage.

Animals↗
PubMed1978

Oxidation-reduction studies of the Mo-(2Fe-2S) protein from Desulfovibrio gigas.

Potentiometric titration followed by e.p.r. measurements were used to determine the midpoint reduction potentials of the redox centres of a molybdenum-containing iron-sulphur protein previously isolated from Desulfovibrio gigas, a sulphate-reducing bacterium (Moura, Xavier, Bruschi, Le Gall, Hall & Cammack (1976) Biochem. Biophys. Res. Commun. 728 782-789; Moura, Xavier, Bruschi, Le Gall & Cabral (1977) J. Less Common Metals 54, 555-562). The iron-sulphur centres could readily be distinguished into three types by means of g values, temperature effect, oxidation-reduction potential values and reduction rates. The type-I Fe-S centres are observed at 77 K. They show mid-point potential values of -260mV (Fe-S type IA) and -440 mV (Fe-S type IB). Centres of types IA and IB appear to have similar spectra at 77 K and 24 K. The Fe-S type-II centres are only observed below 65 K and have a midpoint potential of -28mV. Long equilibration times (30 min) with dye mediators under reducing conditions were necessary to observe the very slow equilibrating molybdenum signals. The potential values associated with this signal were estimated to be approx. -415 mV for Mo(VI)/Mo(V) and-530mV for Mo(V)/Mo(IV).

Desulfovibrio↗
PubMed1980

Energy status and oxidation-reduction status in rat liver at high altitude (3.8 km).

Adult male rats were exposed to 3.8-km altitude for intervals ranging from 1 h-60 d. Liver samples were taken under light ether anesthesia and were examined by enzymatic analyses. Within 1-6 h of hypoxic exposure, ATP levels decreased while ADP and AMP levels increased, producing a fall in calculated ATP/ADP and adenylate charge ratios. Concurrently, lactate/pyruvate and alpha-glycerophosphate/dihydroxyacetone phosphate ratios increased markedly. Direct measurements of cellular pyridine nucleotides indicated increased NADH/NAD and NADPH/NADP ratios. Levels of total adenosine phosphates and pyridine nucleotides decreased in a significant accompanying response. Many metabolite levels and calculated ratios returned to near-normal values within 1 week of exposure, indicating secondary intracellular adjustments to hypoxic stress; however, persistence of that stress is reflected in lactate concentrations and both substrate redox ratios. Results support and explore concepts that increased oxidation-reduction status and decreased energy status are primary events during hypoxia.

Adenosine Diphosphate↗
PubMed1974

Equilibrium relations between the oxidation-reduction reactions and the adenosine triphosphate synthesis in suspensions of isolated liver cells.

1. The redox state of cytochrome c, cytochrome a and the mitochondrial NAD couple, and the phosphorylation state of the adenine nucleotides, were measured in suspensions of isolated rat liver cells. 2. The DeltaG for the transfer of two electrons from the mitochondrial NAD to the cytochrome c couple is calculated to be 104kJ (24.8kcal). 3. The DeltaG associated with the synthesis of ATP at the measured phosphorylation state is calculated to be 95kJ (22.7kcal)/2mol of ATP. 4. The near equality of DeltaG of the electron-transport process and DeltaG required for ATP synthesis indicates near-equilibrium between the mitochondrial respiratory chain and the extramitochondrial phosphorylation state. 5. The existence of near-equilibrium in the coupled reactions implies that the respiratory activity depends on the ratio [ATP]/[ADP][P(i)] and not on the concentrations of the individual reactants. 6. If the overall system of oxidative phosphorylation is at near-equilibrium, all intermediary reactions must also be at equilibrium. Hence if the intramitochondrial and extramitochondrial phosphorylation states are indeed different, it follows that any differences in the activities of ATP, ADP and P(i) must be coupled to ion gradients and/or potentials across the inner mitochondrial membrane in such a way that translocation occurs without loss of free energy. 7. The metabolic state of the mitochondria in the cell can be defined by the turnover number of the cytochromes, the cytoplasmic phosphorylation state, and the oxidation-reduction potential of the NAD couple, rather than by the availability of ADP, substrate and O(2).

Acetoacetates↗
PubMed1982

Streptonigrin toxicity in Escherichia coli: oxygen dependence and the role of the intracellular oxidation--reduction state.

The bacterial physiology of streptonigrin toxicity was further investigated. An optimal oxygen concentration for toxicity was inferred from data showing that streptonigrin at 5 micrograms/mL was rapidly lethal to aerobic cultures of Escherichia coli K12JF361, but was without effect on anaerobic cultures and was bacteriostatic to cultures inhibited in 5 atm of oxygen plus 1 atm of air (5 atm O2 plus air) (1 atm = 101.325 kPa). Escherichia coli were protected from a potentially lethal concentration of streptonigrin during anaerobic incubation, whether previously grown anaerobically, aerobically, or in 5 atm O2 plus air. Superoxide dismutase activity increased with increasing oxygen tension in the medium, but was not significantly changed by a lethal concentration of streptonigrin. Although the superoxide dismutase activity was four times greater in E. coli grown in 5 atm O2 plus air than those grown in air alone, the aerobic survival in 5 micrograms/mL streptonigrin was identical, which suggested that superoxide dismutase was not rate limiting for toxicity. Escherichia coli K12 strains deficient in glutathione (KMBL54-129, AB1157-821, and AB1157-830) were protected from streptonigrin poisoning. Dithiothreotol (5.0 mM), diamide (1 mM), methyl viologen (1 mM), and cyanide (10 mM) protected aerobic E. coli from 5 micrograms/mL streptonigrin. These data are also consistent with a model of in vivo streptonigrin toxicity that requires a favorable intracellular oxidation--reduction state and an optimal concentration of molecular oxygen.

Cells, Cultured↗
PubMed2002

Oxidation-reduction (redox) controls fetal hypoplastic lung growth.

INTRODUCTION: The persistent morbidity and mortality of congenital diaphragmatic hernia are largely due to associated pulmonary hypoplasia. We have shown previously that three antioxidants (vitamin C, glutathione, and vitamin E) could accelerate the growth of fetal hypoplastic lungs grown in culture. We hypothesize that this occurs via a reductant mechanism. METHODS: Timed-pregnant rats were gavage-fed nitrofen (100 mg) on day 9.5 of gestation (term = day 22). Fetal lungs were harvested on day 13.5 and placed in organ culture containing serum-free BGJb medium with antibiotics. After randomization, the lung organ cultures were divided into a control group (n = 31) and an experimental group that received the antioxidant N-acetylcysteine (NAC, 100 microM, n = 31). The fetal lung organ cultures were grown for 4 days at 37 degrees C with 5% CO(2). Computer-assisted digital tracings of the airways were performed daily on live, unstained specimens, and lung bud count, perimeter, and area were measured. After 4 days, lungs were pooled, homogenized, and assayed for reduced and oxidized glutathione, normalized to protein, as an estimate of the tissue redox potential. Data were expressed as means +/- SEM, and statistical comparisons were performed using Student's unpaired t test, with P < 0.05 considered significant. RESULTS: Area, perimeter, lung bud count, and complexity (as measured by the perimeter/square root of area) were all significantly increased with NAC treatment from day 2 onward. Reduced glutathione levels were significantly increased following NAC administration (67.1 +/- 5.8 versus 37.5 +/- 4.2 micromol/mg, P = 0.0004). The ratio of reduced to oxidized glutathione was 2.23. CONCLUSIONS: N-Acetylcysteine stimulates nitrofen-induced hypoplastic fetal lung growth in organ culture and increases the ratio of reduced to oxidized glutathione. These data support the concept that oxidation-reduction (redox) may be an important control mechanism for fetal lung growth.

Acetylcysteine↗
PubMedDate not supplied

pH and oxidation-reduction potential control strategy for optimization of nitrogen removal in an alternating aerobic-anoxic system.

An alternating aerobic and anoxic (AAA) system is a continuous-flow, activated-sludge process in which the environmental conditions necessary to meet the specific requirements for aerobic nitrification and anoxic denitrification are created. Because of stricter regulations on wastewater effluent and concerns on energy consumption, the process control of the system is now becoming more important. A bench-scale AAA system with different fixed aeration ratios was operated for more than 8 months to evaluate effects of the total cycle time and aeration ratio on the system performance and to develop a feasible control scheme. With supplemental organic addition, the system shows removal efficiencies of 85 to 90% and 78 to 82% for chemical oxygen demand and total nitrogen, respectively. The oxidation-reduction potential (ORP) and pH profiles indicate that the aerobic cycle can be controlled by a control point (ammonia valley) on the pH profile indicating the end of nitrification and the anoxic cycle controlled by another point (nitrate knee) on the ORP profile signifying the end of denitrification. Thus, a dual control strategy with the pH and ORP control points was used for terminating aerobic-anoxic and initiating anoxic-aerobic cycles in an AAA system. The performance of the online control system is excellent, with a significant energy saving (average aeration ratio, fa = 0.23) as compared to the fixed time systems (fa = 0.33 to approximately 0.5).

Ammonia↗