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At least 937 records · Page 52Linked to original sources
PubMed1994

[The effect of the composition of an artificial gas environment under pressure up to 5.1 MPa on the oxidation-reduction reactions in the human body].

In 500-m dives, lipid and carbohydrate metabolism was found to depend on the composition of hyperbaric gas mixture. Reduction of the oxygen partial pressure for over 2.0 kPa from the optimal one depressed aerobic energy-producing biochemical reactions in the human blood cells. 5 per cent of nitrogen in the hyperbaric gas mixture at 5.1 MPa suppressed the aerobic metabolism.

Air Pressure↗
PubMed1982

[Role of vanadium in regulation of oxidation-reduction reactions in membranes].

The effect of vanadium on the microsomal membrane system of rat brain and heart was studied. The results obtained exclude the involvement of vanadium in redox processes occurring in brain microsomes. In heart microsomes vanadium, being a redox agent, can control important processes of heart metabolism, while NADH-vanadate-reductase may be a very effective regulator of local pH in heart intracellular membrane systems.

Animals↗
PubMed2002

Oxidation-reduction potential (ORP) regulation of nutrient removal in activated sludge wastewater treatment plants.

Redox potential (ORP) regulation of nutrient removal in aeration tanks was tested for one year in three activated sludge wastewater treatment plants in Cincinnati, OH. The experiment results show a good relationship between ORP values and nutrient removal. Macro-biodegradation and sorption of substrate by activated sludge can significantly increase wastewater ORP, indicating the improvement of redox status of the bulk liquor. DO higher than 1.0 mg/L is necessary for good biodegradation and the improvement of liquid redox status. ORP values at higher temperatures (Twater = 20-26 degrees C) were lower than ORP values at lower temperatures (Twater = 14-19 degrees C), caused by the lower oxygen saturation capacity in wastewater and the more rapid oxygen consumption by microorganism under warmer conditions. Nitrification occurred at higher ORP values (380 mV) than did organic substrate oxidation (250 mV). This verifies that different metabolic processes dominate in different ORP ranges. The pilot-scale experiment results demonstrate that the wastewater ORP values continued to increase throughout the whole 6-hour cycle when the influent COD was higher than 1,000 mg/L. For influent with low COD (40-120 mg/L), the wastewater ORP values did not increase in the second 3 hours of the cycle, during which time the microbial-biodegradation within the activated sludge floc dominated. High DO concentrations (6-8 mg/L) did not help improve the redox status. In fully-aerated wastewater, oxygen deeply penetrated into the activated sludge flocs, and microorganisms biodegraded the substrates within the flocs. Endogenous metabolism predominated.

Biodegradation, Environmental↗
PubMed1975

[Effect of nivaline on some links in the oxidation-reduction and energy processes in striated and cardiac muscles].

The authors examined the effect of nivaline on the oxyreductive and energetic processes in the striated and smooth muscles under the conditions of a laboratory experiment. After determining the changes occurred in the succinatdehydrogenase, glutamat-dehydrogenase, glutamat-oxalacetic and glutamat-pyruvic transaminases, adenosinotriphosphate and adenosinemonophosphate, the authors found that nivaline enhanced oxyreuctive and energetic processes, connected with accumulation of adenosintriphosphate, which abolished quickly the fatique.

Animals↗
PubMed1981

On the relationship between the uncoupler-induced efflux of K+ from heart mitochondria and the oxidation-reduction state of pyridine nucleotides.

Respiring heart mitochondria exchange matrix 42K+ with extramitochondrial K+ at a rapid rate in the presence of Pi (Chávez, E., Jung, D. W., and Brierley, G. P. (1977) Arch. Biochem. Biophys. 183, 460-470, 1977). This exchange reaction is strongly inhibited by uncouplers. However, under two rather similar sets of conditions, the addition of an uncoupler results in a rapid, transient increase in the exchange of matrix 42K+ with external K+ when the mitochondria are suspended in KCl or, alternatively, in a net loss of matrix 42K+ from mitochondria suspended in K+-free media. These conditions are: (a) the addition of an uncoupler to respiring mitochondria after the accumulation of a small amount of phosphate salt, and (b) the presence of a Ca2+-chelator or ruthenium red with uncoupler. Loss of 42K+ under these conditions occurs with all substrates tested, is completely blocked by rotenone, and is accompanied by an almost complete oxidation of both NADH and NADPH. In the presence of rotenone and acetoacetate, only NADH is oxidized and 42K+ efflux does not occur. It is concluded that simply dissipating the mitochondrial protonmotive force by addition of an uncoupler is not sufficient to induce release of mitochondrial K+. Uncoupler-induced oxidation of mitochondrial NADPH, in conjunction with elevated internal Pi, opens a rather nonspecific pathway for K+ loss which can be inhibited by ADP and enhanced by Ca2+. The more specific loss of K+ which occurs in the absence of elevated internal Pi when uncoupler and EGTA or ruthenium red are present suggests that K+ efflux is related to the Ca2+-uniporter. Loss of K+ by either of these pathways can be differentiated from efflux of K+ on the endogenous K+/H+ exchanger which functions without dissipation of the mitochondrial membrane potential.

Animals↗
PubMed1973

Capacitor electrode stimulates nerve or muscle without oxidation-reduction reactions.

Porous tantalum disks, available as "slugs" from the capacitor industry, have large available surface area and a thin insulating coating of tantalum pentoxide. When implanted, they fill with extracellular fluid and operate as capacitor-stimulating electrodes having high capacitance per unit volume. Capable of stimulating excitable tissute without generating electrochemical by-products, these electrodes should provide a safer interface between neural prosthetic devices and human tissue.

Animals↗
PubMed1992

Oxidation-reduction-sensitive binding of lung protein to rat catalase mRNA.

Air-breathing organisms experience an elevated concentration of oxygen mainly under two conditions. One occurs at birth when the O2 tension in the lung increases from approximately 25 torr present in utero to approximately 100 torr. The lungs, in particular, are also exposed to hyperoxia when oxygen is administered for therapeutic reasons. Under hyperoxic conditions, increased lung antioxidant enzyme activity is important for survival. The molecular basis for the increase in antioxidant enzyme gene expression under these circumstances is not well understood; in hyperoxia-exposed neonatal rats the elevation of lung catalase activity is not due to an increased rate of transcription but is associated with an increased concentration of catalase mRNA due to enhanced stability of the mRNA (Clerch, L.B., Iqbal, J., and Massaro, D. (1991) Am. J. Physiol. 260, L428-L433). We now show that neonatal rat lung protein forms specific complexes with catalase mRNA; this binding is redox-sensitive since when oxidizing agents are added binding is abolished but is restored by reducing agents. Our data also indicate lungs from hyperoxia-exposed rats have a larger proportion of catalase RNA-binding protein in oxidized form than lungs from air-breathing rats. This redox-sensitive binding of protein to catalase mRNA may be important in the control of catalase gene expression.

Aging↗
PubMed1977

Oxidation--reduction potentials of turkey liver xanthine dehydrogenase and the origins of oxidase and dehydrogenase behaviour in molybdenum-containing hydroxylases.

Redox potentials for the various centres in the enzyme xanthine dehydrogenase (EC 1.2.1.37) from turkey liver determined by potentiometric titration in the presence of mediator dyes, with low-temperature electron-paramagnetic-resonance spectroscopy. Values at 25 degrees C in pyrophosphate buffer, pH 8.2, are: Mo(VI)/Mo(V)(Rapid),-350 +/- 20mV; Mo(V) (Rapid)/Mo(IV), -362 +/- 20mV; Fe-S Iox./Fe-S Ired., -295 +/- 15mV; Fe-S IIox./Fe-S IIred., -292 +/- 15mV; FAD/FADH,-359+-20mV; FADH/FADH2, -366 +/- 20mV. This value of the FADH/FADH2 potential, which is 130mV lower than the corresponding one for milk xanthine oxidase [Cammack, Barber & Bray (1976) Biochem. J. 157, 469-478], accounts for many of the differences between the two enzymes. When allowance is made for some interference by desulpho enzyme, then differences in the enzymes' behaviour in titration with xanthine [Barber, Bray, Lowe & Coughlan (1976) Biochem. J. 153, 297-307] are accounted for by the potentials. Increases in the molybdenum potentials of the enzymes caused by the binding of uric acid are discussed. Though the potential of uric acid/xanthine (-440mV) is favourable for full reduction of the dehydrogenase, nevertheless, during turnover, for kinetic reasons, only FADH and very little FADH2 is produced from it. Since only FADH2 is expected to react with O2, lack of oxidase activity by the dehydrogenase is explained. Reactivity of the two enzymes with NAD+ as electron acceptor is discussed in relation to the potentials.

Animals↗
PubMed1996

Polycyclic aromatic hydrocarbon quinone-mediated oxidation reduction cycling catalysed by a human placental 17beta-hydroxysteroid dehydrogenase.

The human placental 17beta-hydroxysteroid dehydrogenase reduces a number of polycyclic aromatic hydrocarbon (PAH) o-quinones; some of the quinones undergo redox cycling at rates that approach or exceed the rate of reduction of estrone by the enzyme. The non-K-region o-quinone, 7,8-benzo[a]pyrenequinone, is the best o-quinone substrate tested. Cycling of all the quinone substrates is inhibited by superoxide dismutase; cycling is also inhibited by 17beta-estradiol and other estrogens. Since 19 alpha-estradiol is a competitive inhibitor of 9,10-phenanthrenequinone by the 17beta-hydroxysteroid dehydrogenase, it is likely that both reactions occur at the same active site on the enzyme. In the presence of the 17beta-hydroxysteroid dehydrogenase, the equilibrium between 17beta-estradiol, estrone, NADP, and NADPH is shifted by 7,8-benzo[a]pyrenequinone because the rapid redox cycling of this quinone results in the oxidation of NADPH. Unlike a number of hydroxysteroid dehydrogenases, the placental 17beta-hydroxysteroid dehydrogenase does not oxidize any of the six PAH trans-dihydrodiols tested.

17-Hydroxysteroid Dehydrogenases↗
PubMed1978

[Microbial metabolic activity and transmembrane transport phenomena by potentiometric analysis of lipoic acid oxidation-reduction, in a minimal culture medium].

A method of measuring and studying metabolic bacterial activity is proposed, by following the kinetic evolution of the ratio of the oxidized and reduced forms of an electron transporter as a consequence of decreasing oxidizing power--due to oxygen consumption in the culture,--and increasing. Reduction power of bacterial activity. Namely, with minimum composition using salts and glucose the oxido-reduction of lipoic acid is well indicated by a gold electrode without any major bio-or electrochemical interference. A kinetic diffusion reaction theory takes into account the passive or active transmembrane transport of lipoic acid in good agreement with the experimentally observed shapes of the electrical signal. The various types of antibiotic activities are well reflected by the modifications of the signal.

Bacteria↗
PubMed1978

Pyridine nucleotide oxidation-reduction state of the cerebral cortex in the awake gerbil.

A new approach to study the effect of ischemia on the brain of the awake gerbil is described. The measurement of NADH fluorescence from the surface of the cortex is done by a time-sharing fluorometer/reflectometer connected to the brain via a flexible light guide and an implanted cannula. The response of the gerbil brain to anoxia and spreading depression is described. By unilateral occlusion of the carotid artery an increase in NADH was measured in the ipsilateral hemisphere.

Animals↗
PubMed1989

[Effect of the oxidation-reduction potential of the medium on the production of gentamycin].

The medium redox potential had an effect on gentamicin production by Micromonospora purpurea v. violacea, strain VNIIA 7R. The Eh influence was shown to be statistically reliable when the results were expressed in relative units against the control. In the laboratory experiments with low volumes of the medium the Eh increase by more than 170 per cent induced inhibition of gentamicin biosynthesis while the Eh increase by 108 to 168 per cent induced stimulation of the activity.

Culture Media↗
PubMedDate not supplied

[The seasonal dynamics of the indices of the oxidative-reductive processes in the erythrocytes of healthy subjects of different ages].

A study is reported of the dynamics of the activity of enzymes markers of different metabolic ways--glycolysis, pentosophosphate cycle, gluconeogenesis--in erythrocytes of 157 practically healthy subjects in two age groups: from 20 to 35 years and from 35 to 60 years. It was shown that seasonal biorhythms of the above values that were definite in the young changed with age. These findings suggest the necessity of a chronobiological approach to research and clinico-laboratory investigations.

Adult↗
PubMed1985

Interflavin oxidation-reduction reactions between pig kidney general acyl-CoA dehydrogenase and electron-transferring flavoprotein.

The mechanism of interflavin electron transfer between pig kidney general acyl-CoA dehydrogenase (GAD) and its physiological acceptor, electron-transferring flavoprotein (ETF), has been studied by static and stopped-flow absorbance and fluorescence measurements. At 3 degrees C, pH 7.6, reoxidation of the dehydrogenase (stoichiometrically reduced by octanoyl-CoA) by ETF is multiphasic, consisting of two rapid phases (t1/2 of about 20 and 50 ms), a slower phase half-complete in about 1 s, and a final reaction with a half-time of 20 s. Only the two most rapid phases are significant in turnover. This complicated reaction course was dissected by examining the rates of plausible individual steps, e.g., GAD2e X P + ETF1e, GAD1e X P + ETFox, and GAD1e X P + ETF1e (where P represents the product, octenoyl-CoA, and the subscripts indicate the redox state of the flavin). Rapid reaction and static fluorescence measurements, in all cases, showed that the final equilibrium mixture included appreciable levels of oxidized ETF. This was confirmed by measuring the reverse reactions, e.g., ETF1e + GADox X P, ETF1e + GAD1e X P, and ETF2e + GADox X P. These data support the following overall scheme for the reaction of GAD2e X P with ETFox: The first and second phases correspond to reoxidation of GAD2e X P in two successive one-electron steps requiring two molecules of ETFox. This results in a rapid rise in absorbance at 370 nm where the red anionic radicals of both product-complexed dehydrogenase and ETF absorb strongly.(ABSTRACT TRUNCATED AT 250 WORDS)

Acyl-CoA Dehydrogenases↗
PubMed1986

Oxidation-reduction properties of glycolate oxidase.

This is the first report of the redox potentials of glycolate oxidase. The pH dependence of the redox behavior as well as the effects of activators and inhibitors was studied. At pH 7.1 in 10 mM imidazole-chloride, Eo1' (EF1ox/EF1-.) is -0.033 +/- 0.010 V and Eo2' (EF1-./EF1redH-) is -0.017 +/- 0.017 V vs. the standard hydrogen electrode at 10 degrees C. A maximum of 29% flavin mononucleotide (FMN) anion radical is stabilized at half-reduction at pH 7.1 and 10 degrees C. Both redox couples of glycolate oxidase are pH-dependent from pH 7 to pH 9, and the FMN anion radical is stabilized in this range. The redox potentials of glycolate oxidase are shifted markedly positive of those of unbound FMN, consistent with the enzyme's function. The midpoint potential of glycolate oxidase is more positive than that of the glyoxalate/glycolate couple, and two-electron reduction of glycolate oxidase is thermodynamically favorable. The redox behavior of glycolate oxidase markedly contrasts that of other flavoprotein oxidases. For most flavoprotein oxidases, Eo1' is independent of pH from pH 7 to pH 9 and is much more positive than Eo2', which is pH-dependent. We present a mechanism that suggests a structural basis for the positive shifts and pH dependence of both Eo1' and Eo2' of glycolate oxidase.

Alcohol Oxidoreductases↗
PubMed1990

[The dynamics of the potential of the oxidative-reductive status of the cerebral cortex developing as a reaction to implanted platinum electrodes].

The dynamics of the ROPS was studied in rabbits with implanted electrodes. Within 5-25 days after the implantation, the ROPS underwent a series of positive and negative oscillations with gradually extinguishing amplitude. The ROPS as recorded with the electrodes implanted in the dura matter shifted on the average to relatively stable negative values whereas the ROPS in the pia matter electrodes and in the brain cortex shifted to positive values, rather.

Animals↗
PubMed2003

Human natural killer cell activity against porcine targets: modulation by control of the oxidation-reduction environment and role of adhesion molecule interactions.

Xenotransplantation, especially using porcine sources, has been proposed as a means to alleviate the shortage of human organs for transplantation. NK cells appear to be important mediators of the xenogeneic immune responses, including the human anti-pig response. Having previously established the redox regulation of NK cell activity against tumor target cells, we now report that the interaction of human NK cells with porcine target cells is also regulated by redox. Thiol-deprivation strongly diminished the capacity of IL-2-activated human NK cells to kill porcine endothelial cells. This inhibition correlated with reduced proliferation and interferon (IFN)-gamma production by IL-2-activated NK cells. For fresh NK cells, pretreatment with diethyl maleate (DEM), which was used to deplete intracellular thiols, reduced lysis of porcine and human targets. Because many adhesion molecules exhibit interspecies recognition, we further investigated whether changes in expression of adhesion molecules might explain our observations. DEM treatment reduced the expression of CD11b and CD29 on fresh NK cells. Monoclonal antibody blocking studies showed that the combination of mAb to CD11b and CD18 reduced lytic activity against both PAEC as well as K562, although other qualitative differences were observed between the porcine and human target cells. These findings suggest that the oxidative stress-induced downregulation of CD18 may be important in modulating cytotoxic activity of fresh NK cells against PAEC and K562 targets through reduced formation of the CD11b/CD18 heterodimer. Thus, the appropriate manipulation of redox status may provide a means to enhance survival of non-human animal tissues in humans through modulation of adhesion molecule expression/interactions.

Animals↗