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PubMed1976

Polarographic studies in presence of Triton X-100 on oxidation-reduction components bound with chromatophores from Rhodospirillum rubrum.

Polarographic studies on oxidation-reduction components bound with chromatophores from Rhodospirillum rubrum were carried out at 24 degrees. 1. Using a carbon-paste electrode as the working electrode, polarographic waves characteristic of oxidation-reduction components were observed in the presence, but not in the absence of Triton X-100; these waves were therefore measured in the presence of the detergent. 2. At least two kinds of oxidation-reduction components were detectable, having different half-wave potentials (E1/2); at pH 7, one had an E1/2 value of +275 mV (POC+275) and the other had a value of +60 mV (POC+60). 3. POC+275 was reduced by succinate and by NADH. Both reductions were almost completely inhibited by antimycin A, which hardly affected the reductions of ubiquinone-10 by succinate and by NADH. Most POC+275 molecules were not reduced by the substrates when quinones were extracted from the chromatophores, and the reductions were mostly restored when ubiquinone-10 was re-added. This indicates that POC+275 is functional between ubiquinone-10 and cytochrome c2 in the electron transport system. 4. POC+60 was reduced by succinate, but hardly at all by NADH. The reduction of POC+60 was not influenced either by the addition of antimycin A or by the extraction of quinones. This suggests that POC+60 is functional in the process from succinate dehydrogenase [EC 1.3.99.1] to ubiquinone-10 in the electron transport system. 5. Of the POC+275 reducible by dithionite, approximately 70% could be reduced in the absence of Triton X-100, provided that the potential of the working electrode immersed in chromatophore suspensions was set at potentials of 0 mV or lower and that the electrochemical reaction was carried out at pH 7.5. When the potential of the electrode was set at +50 mV (the same as the E1/2 value of ubiquinone-10 bound with chromatophores), and the suspension was allowed to stand for various lengths in the presence of the detergent, it was found that approximately half of the electrochemically reducible POC+275 was rapidly reduced, followed by a slow reduction. The discrepancy in the oxidation-reduction equilibrium on the basis of the E1/2 values of ubiquinone-10 and POC+275 is discussed.

Antimycin A↗

PubMed2003

Effect of pH on the oxidation-reduction properties of thioredoxins.

Oxidation-reduction midpoint potential (E(m)) versus pH profiles were measured for wild-type thioredoxins from Escherichia coli and from the green alga Chlamydomonas reinhardtii and for a number of site-directed mutants of these two thioredoxins. These profiles all exhibit slopes of approximately -59 mV per pH unit, characteristic of the uptake of two protons per reduction of an active-site thioredoxin disulfide, at acidic, neutral, and moderately alkaline pH values. At higher pH values, these profiles exhibit slopes of either -29.5 mV per pH unit, characteristic of the uptake of one proton per disulfide reduced, or are pH-independent, indicating that neither proton uptake nor proton release is associated with reduction of the active-site disulfide. Reduction of the two wild-type thioredoxins is accompanied by the uptake of two protons even at pH values where the more acidic cysteine thiol group of the reduced proteins would be expected to be completely unprotonated. The effect of site-directed mutagenesis of two highly conserved aspartate residues that play important structural and/or catalytic roles in both thioredoxins, and which could in principle play a role in proton transfer, on the pK(a) values of redox-linked acid dissociations (deduced from changes in slope of the E(m) versus pH profiles) has also been determined for both E. coli thioredoxin and C. reinhardtii thioredoxin h.

Alanine↗

PubMed1981

The relation of pH and oxidation-reduction potential to the association state of the ferredoxin . ferredoxin:NADP+ reductase complex.

The interaction between spinach ferredoxin and ferredoxin:NADP+ reductase was studied by varying pH and oxidation-reduction state. The Kd of the oxidized ferredoxin . ferredoxin:NADP+ reductase complex increases with increasing pH in the range from pH 6 to pH 8; the Kd is pH-independent above pH 9. These data are interpreted as showing 1 proton binding/complex at neutral pH. The extent of association of the complex was also varied by manipulation of salt concentration, was also varied by manipulation of salt concentration, and of concentration of the individual proteins. Increased association accompanied a negative shift in potential of ferredoxin relative to that of ferredoxin: NADP+ reductase. Oxidation-reduction titrations showed that the oxidation-reduction potential of ferredoxin is reduced to above -510 mV when in complex with ferredoxin:NADP+ reductase, a change of about -90 mV; the potential of ferredoxin:NADP+ reductase is changed little (no more than +20 mV). Conversely, these data also showed that the oxidation-reduction state of ferredoxin strongly affected its association with the flavoprotein, increasing the Kd at least 30-fold on reduction of ferredoxin.

Ferredoxin-NADP Reductase↗

PubMed1976

Measurement of the oxidation-reduction potentials for two-electron and four-electron reduction of lipoamide dehydrogenase from pig heart.

The oxidation-reduction potential, E2, for the couple oxidized lipoamide dehydrogenase/2-electron reduced lipoamide dehydrogenase has been determined by measurement of equilibria of these enzyme species with lipoamide and dihydrolipoamide or with oxidized and reduced azine dyes. E2 is -0.280 V at pH 7, and deltaE2/deltapH is -0.06 V in the pH range 5.5 to 7.6. Values for E1, the oxidation-reduction potential for the couple 2-electron reduced enzyme/4-electron reduced enzyme, were obtained from measurements of the extent of dismutation of 2-electron reduced enzyme to form mixtures containing oxidized and 4-electron reduced enzyme. E1 is -0.346 V at pH 7, and deltaE1/deltapH is -0.06 V in the pH range 5.7 to 7.6. Spectra of oxidized enzyme and 4-electron reduced enzyme do not show variations with pH over this range, but the spectrum of the 2-electron reduced enzyme is pH-dependent, with the molar extinction at 530 nm changing from 3250 M-1 cm-1 at pH 8 to 2050 M-1 cm-1 at pH 5.2. The pH-dependent changes which are observed in the absorption properties of the 2-electron reduced enzyme are consistent with the disappearance of a charge transfer complex between an amino acid side chain and the oxidized flavin at the lower pH values, with the apparent pK of the side chain at pH 5. It has been suggested that the 530 nm absorbance of 2-electron reduced enzyme is due to a charge transfer complex between thiolate anion and oxidized flavin, and we propose that the thiolate anion is stabilized by interaction with a protonated base. The thermodynamic data predict that the amount of 4-electron reduced enzyme formed when the enzyme is reduced by excess NADH will be pH-dependent, with the greatest amounts seen at low pH values. These data support earlier evidence (Matthews, R.G., Wilkinson, K.D., Ballou, D,P., and Williams, C.H., Jr. (1976) in Flavins and Flavoproteins (Singer, T.P., ed) pp. 464-472; Elsevier Scientific Publishing Co., Amsterdam) that the role of NAD+ in the NADH-lipoamide reductase reaction catalyzed by lipoamide dehydrogenase is to prevent accumulation of inactive 4-electron reduced enzyme by simple reversal of the reduction of 2-electron reduced enzyme by NADH.

Animals↗

PubMed1976

The correlation between salivary peroxidase activity, salivary flow rate, and the oxidation-reduction potentials of human saliva and dental plaque suspensions.

18 subjects, 9 males and 9 females, were examined regarding salivary oxidation-reduction potential, salivary flow rate, salivary peroxidase activity, oxidation-reduction potential of dental plaque samples, and dental health. Both the peroxidase activity, expressed as the salivary lactoperoxidase, and the salivary oxidation-reduction potential increased with increasing salivary flow rate. The variation of these variables was obviously due to changes in salivary flow rate during the day. The remarkably slight differences in peroxidase activities, oxidation-reduction potentials and salivary flow rate in this study did not have any marked correlation with the clinical recordings of the test groups.

Adult↗

PubMed2003

Use of ORP (oxidation-reduction potential) to control oxygen dosing for online sulfide oxidation in anaerobic treatment of high sulfate wastewater.

In this study, oxidation-reduction potential (ORP) was used as a controlling parameter to regulate oxygen dosing to the recycled biogas for online sulfide oxidation in an upflow anaerobic filter (UAF) system. The UAF was operated with a constant influent COD of 18,000 mg/L, but with different influent sulfates of 1000, 3000 and 6000 mg/L. The reactor was initially operated under a natural ORP of -290 mV (without oxygen injection), and was then followed by oxygenation to raise its ORP by 25 mV above the natural level for each influent sulfate condition. At 6,000 mg/L sulfate without oxygen injection, the dissolved sulfide reached 733.8 mg S/L with a corresponding free sulfide of 250.3 mg S/L, thus showing a considerable inhibition to methanogens. Upon oxygenation to raise its ORP to -265 mV (i.e., a 25 mV increase), the dissolved sulfide was reduced by more than 98.5% with a concomitant 45.9% increase of the methane yield. Under lower influent sulfate levels of 1,000 and 3,000 mg/L, the levels of sulfides produced, even under the natural ORP, did not impose any noticeable toxicity to methanogens. Upon oxygenation to raise the ORP by +25 mV, the corresponding methane yields were actually reduced by 15.5% and 6.2%, respectively. However, such reductions were not due to the adverse impact of the elevated ORP; instead, they were due to a diversion of some organic carbon to support the facultative activities inside the reactor as a result of excessive oxygenation. In other words, to achieve satisfactory sulfide oxidation for the lower influent sulfate conditions, it was not necessary to raise the ORP by as much as +25 mV. The ORP increase actually needed depended on both the influent sulfate and also actual wastewater characteristics. This study had proved that the ORP controlled oxygenation was reliable for achieving consistent online sulfide control.

Automation↗

PubMed1999

Molecular and cellular responses to oxidative stress and changes in oxidation-reduction imbalance in the intestine.

Recently, it has become increasingly apparent that oxidants, in addition to being agents of cytotoxicity, can play an important role in mediating specific cell responses and expression of genes involved in degenerative pathophysiologic states, such as inflammation and cancer. In particular, nuclear transcription factor kappaB (NF-kappaB), a multisubunit transcription factor, has been implicated in the transcriptional up-regulation of inflammatory genes in response to oxidants or changes in cellular oxidation-reduction status. This paper provides an overview of the cellular responses to oxidative stress and oxidation-reduction imbalance and the role of NF-kappaB in these responses and summarizes the current strategies used to study NF-kappaB activation and nuclear translocation, particularly in relation to dietary oxidant-mediated pathophysiology of the intestine.

Cell Transformation, Neoplastic↗

PubMed1968

Monitored environment system to control cell growth, morphology, and metabolic rate in fungi by oxidation-reduction potentials.

A device for the adjustment, maintenance, and monitoring of a desired oxidation-reduction potential in a liquid environment is described. The filamentous species, Penicillium lilacinum and Trichophyton schoenleinii, and the dimorphic species, Histoplasma capsulatum, developed budding yeastlike cells when grown in a liquid medium with a low oxidation-reduction potential. When the organisms were inoculated into fresh medium, they returned to the filamentous condition as the oxidation-reduction potential was restored to a more positive (oxidizing) environment.

Candida↗

PubMed1976

Oxidation-reduction properties of Chromatium vinosum high potential iron-sulfur protein.

The oxidation-reduction properties of the high potential iron-sulfur protein (HIPIP) from Chromatium vinosum have been investigated. Both equilibrium and kinetic measurements demonstrate electron transport by HIPIP is pH independent in the pH range 7-11. The kinetics of reduction (potassium ferrocyanide, SO2, S2O42-, sodium ascorbate, and Rhodospirillum rubrum cytochrome c2) and oxidation (potassium ferricyanide and Rhodospirillium rubrum cytochrome c2) of HIPIP are reported. Based on the data obtained with different reactants and the influence of ionic strength, pH, and temperature on the kinetics of oxidation and reduction, a number of conclusions can be drawn. (1) HIPIP undergoes rapid outer-sphere electron transfer with no evidence of kinetic complexity and no indication of complex formation with various reactants. (2) The site of oxidation of reduced HIPIP has an apparent negative charge while the site of reduction of oxidized HIPIP is uncharged. (3) HIPIP appears to interact with a physiological reactant (R. rubrum cytochrome c2) at the same site as nonphysiological oxidants or reductants suggesting single minimum energy pathways for the oxidation and reduction processes. (4) Based on a comparison of the rates of oxidation and reduction with different reactants, it appears that steric restrictions and differences in oxidation-reduction potential are less important than electrostatic attraction and/or repulsion in determining the absolute rate constants. (5) The thermodynamic activation parameters indicate that both oxidation and reduction by the iron hexacyanides are driven entropically with the enthalpic terms making no contribution to HIPIP oxidation and a small contribution to HIPIP reduction. Based on the data reported here and available structural and physical-chemical information, possible mechanisms of the oxidation and reduction of HIPIP are discussed and their relative merits analyzed. The more likely mechanisms include electron transfer via a tyrosine residue, electron transfer through a nonaqueous media to the iron-sulfur chromophore, and direct interaction between the iron-sulfur chromophore and the different oxidants and reductants.

Binding Sites↗

PubMed1985

The rate of protein degradation in isolated skeletal muscle does not correlate with reduction-oxidation status.

It has been suggested that the cytoplasmic reduction-oxidation state correlates with, and may regulate, rates of protein breakdown in skeletal muscle. To test whether an increased lactate/pyruvate ratio is in fact generally associated with low proteolytic rates, this ratio was measured in rat extensor digitorum longus muscles incubated under conditions that rates of protein breakdown. Treatment with the calcium ionophore A23187 caused similar large increases in the lactate/pyruvate ratio at 2 microM, where proteolysis did not change, and at 20 microM, where proteolysis was greatly accelerated. Omission of Ca2+ from the medium slowed proteolysis, but decreased the lactate/pyruvate ratio. In muscles incubated at 40 degrees C, rates of proteolysis were faster, but the lactate/pyruvate ratios were higher than 37 degrees C. Thus alterations in the redox status do not necessarily correlate with, and can occur independently of, changes in proteolysis. Furthermore, insulin and inhibitors of lysosomal proteinases decreased proteolysis but, in contrast with previous reports, failed to alter the lactate/pyruvate ratio. In addition, protein breakdown decreased in muscles maintained under tension, although redox state did not change. Thus protein degradation can fall without a concomitant change in the reduction-oxidation state.

Animals↗

PubMed1998

Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation.

Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation were investigated. Glycation of bovine serum albumin by methylglyoxal generated the protein-bound free radical, probably the cation radical of the cross-linked Schiff base, as observed in the reaction of methylglyoxal with L-alanine (Yim, H.-S., Kang, S.-O., Hah, Y. C., Chock, P. B., and Yim, M. B. (1995) J. Biol. Chem. 270, 28228-28233) or with Nalpha-acetyl-L-lysine. The glycated bovine serum albumin showed increased electrophoretic mobility suggesting that the basic residues, such as lysine, were modified by methylglyoxal. The glycated protein reduced ferricytochrome c to ferrocytochrome c in the absence of oxygen or added metal ions. This reduction of cytochrome c was accompanied by a large increase in the amplitude of the electron paramagnetic resonance signal originated from the protein-bound free radical. In addition, the glycated protein catalyzed the oxidation of ascorbate in the presence of oxygen, whereas the protein free radical signal disappeared. These results indicate that glycation of protein generates active centers for catalyzing one-electron oxidation-reduction reactions. This active center, which exhibits enzyme-like characteristic, was suggested to be the cross-linked Schiff base/the cross-linked Schiff base radical cation of the protein. It mimics the characteristics of the metal-catalyzed oxidation system. The glycated bovine serum albumin cross-linked further to the cytochrome c in the absence of methylglyoxal. The cross-linked cytochrome c maintains its oxidation-reduction properties. These results together indicate that glycated proteins accumulated in vivo provide stable active sites for catalyzing the formation of free radicals.

Ascorbic Acid↗

PubMedDate not supplied

Isolation and characterization of glutathione reductase from Physarum polycephalum and stage-specific expression of the enzyme in life-cycle stages with different oxidation-reduction levels.

Physarum polycephalum has a life cycle with several distinct phases that have different oxidation-reduction requirements. To investigate the relationship between the life cycle and the oxidation-reduction state, we isolated glutathione reductase (GR; EC 1.6.4.2) from Physarum microplasmodia. The enzyme was found to be a homodimer with a subunit M(r) of 49,000, and K(m) values for oxidized glutathione and NADPH of 40 and 28.6 microM, respectively. We then constructed a cDNA library from microplasmodium mRNA and cloned GR cDNA from the library. The isolated cDNA consisted of 1,475 bp encoding a polypeptide of 452 amino acids. The amino acid sequence similarity was about 50% with GRs of other organisms, and several conserved sequence motifs thought to be necessary for activity are evident in the Physarum enzyme. Escherichia coli transformed with an expression vector containing the cDNA synthesized the active GR. Genomic Southern blot analysis indicated that the GR gene is present as a single copy in the Physarum genome. Immunoblot analysis and RT-PCR analysis detected GR mRNA expression in the microplasmodium, plasmodium, and sclerotium, but not in the spore or flagellate. GR activity was low in the spore and flagellate. These results suggest that the glutathione oxidation-reduction system relates to the Physarum life cycle.

Amino Acid Sequence↗

PubMed1976

pH dependence of the oxidation-reduction potential of cytochrome c2.

The pH dependence of the spectra and of the oxidation-reduction potential of three cytochromes c2, from Rhodopseudomonas capsulata, Rhodopseudomonas sphaeroides and Rhodomicrobium vannielii, were studied. A single alkaline pK was observed for the spectral changes in all three ferricytochromes. In Rps. capsulata cytochrome c2 this spectroscopic pK corresponds to the pK observed in the dependence of oxidation-reduction potential on pH. For the other two cytochromes the oxidation-reduction potential showed a complex dependency on pH which can be fitted to theoretical curves involving three ionizations. The third ionization corresponds to the ionization observed in the spectroscopic studies but the first two occur without changes in the visible spectra. The possible structural bases for these ionizations are discussed.

Cytochrome c Group↗

PubMed1965

STUDIES ON THE OXIDATION-REDUCTION POTENTIALS OF HEME PROTEINS. V. THE OXIDATION BOHR EFFECT IN NORMAL HUMAN HEMOGLOBIN AND HUMAN HEMOGLOBIN DIGESTED WITH CARBOXYPEPTIDASE A.

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Carboxypeptidases↗

PubMed1982

Extended X-ray absorption fine structure studies of cytochromes c: structural aspects of oxidation-reduction.

EXAFS fluorescence spectra were recorded for high-potential c-type cytochromes which range in oxidation-reduction potential from +145 to +365 mV. No average Fe-ligand bond length differences greater than 0.03 A were observed, for any cytochrome source of oxidation state. Least-squares analysis in combination with model calculations allowed limits to be set on the average Fe-N bond length (1.97-1.99 A) and the Fe-S bond length (2.29-2.32 A). A change of 0.05 A in either the average Fe-N or the Fe-S bond length is readily detectable with the range and quality of the data presented here. Two major conclusions are drawn from this study: In octahedrally coordinated iron porphyrin systems, Fe-N and Fe-S bond lengths are independent of oxidation-reduction potential, and they are also independent of oxidation state. A model for the regulation of oxidation-reduction potential in cytochrome c is proposed.

Animals↗

PubMed2005

Transcriptional regulation of nitric oxide reduction in Ralstonia eutropha H16.

Nitric oxide reduction in Ralstonia eutropha H16 is catalysed by the quinol-dependent NO reductase NorB. norB and the adjacent norA form an operon that is controlled by the sigma(54)-dependent transcriptional activator NorR in response to NO. A NorR derivative containing MalE in place of the N-terminal domain binds to a 73 bp region upstream of norA that includes three copies of the putative upstream activator sequence GGT-(N(7))-ACC. Mutations altering individual bases of this sequence resulted in an 80-90% decrease in transcriptional activation by wild-type NorR. Similar motifs are present in several proteobacteria upstream of genes encoding proteins of NO metabolism. The N-terminal domain of NorR contains a GAF module and is hypothesized to interact with a signal molecule. A NorR derivative lacking this domain activates the norAB promoter constitutively. Amino acid exchanges within the GAF module identified a cysteine residue that is essential for promoter activation by NorR. Signal sensing by NorR is negatively modulated by the iron-containing protein NorA.

Catalysis↗

PubMed2001

Relationship between release of nitric oxide and CO2 and their dependence on oxidation reduction potential in wastewater treatment.

Nitric oxide (NO) is an intermediate of denitrification process and can be produced by denitrifiers, nitrifiers and other bacteria. In our experiments we measured the dynamic flow of NO depending on oxidation reduction potential (ORP). Different ORP-ranges were related to various carbon loading stages in the wastewater treatment pilot plant. Nitrification and denitrification were achieved by a sequence of aeration and non-aeration periods. Our measurements show that different carbon loading conditions (low feed, balanced and overloaded conditions) did not change the range of the mixing ratio of NO emissions when the aeration conditions like air-flow and temperature were kept constant. Minimum and maximum NO mixing ratios were 34.7 and 91.8 ppbv; 52.3 and 91.3 ppbv; 57.6 and 109 ppbv for low feed, balanced and overloaded conditions, respectively. The curve of the NO graph relied on nitrification/denitrification dynamics. The dependence of NO release on different ORP and CO2-release during the various conditions are shown. Longer aeration times resulted in an increased release of gaseous NO. The net-release of NO g(-1) nitrogen removed was between 0.014% and 0.028%. The NO fluxes to the air were observed between 8.3 and 14.9 mg m(-2) d(-1) NO. The major release occurred during high aeration periods whereas the concentration of dissolved [NOaq] in the wastewater was less than 0.05% of the gaseous release due to very low solubility of the NO.

Air Pollutants↗

PubMed1990

Chemical change involved in the oxidative reductive depolymerization of hyaluronic acid.

The oxidative reductive depolymerization (ORD) of hyaluronate has been investigated. A solution of hyaluronate (Mr 4.07 x 10(5] in phosphate buffer (pH 7.2) was incubated in the presence of Fe2+ for 24 h at 37 degrees C under an oxygen atmosphere to yield depolymerized hyaluronate (ORD fragments; an average Mr of 2,600). The ORD fragments contain 21 and 24% less hexosamine and uronic acid, respectively, but no olefinic linkage. They were exhaustively digested with chondroitinase AC-II. The resulting oligosaccharides and monosaccharides were separated by gel filtration and ion-exchange chromatography, and their structures were determined by proton and carbon-13 NMR, fast atom bombardment mass spectrometry, and chromatographic techniques combined with chemical modifications. The following structures derived from the reducing ends of the ORD fragments were identified: 4,5-unsaturated GlcA(beta 1----3)-N-acetyl-D-glucosaminic acid (where GlcA- represents glucuronosyl-) (21%), 4,5-unsaturated GlcA(beta 1----3)GlcNAc(beta 1----3)-D-arabo-pentauronic acid (24%), and N-acetyl-D-glucosamine (51%). The following structures derived from the nonreducing ends were identified: L-threo-tetro-dialdosyl-(1----3)GlcNAc (a tentative structure, 8%), N-acetylhyalobiuronic acid (20%), and N-acetyl-D-glucosamine (45%). The results indicate that the ORD reaction of hyaluronate proceeds essentially by random destruction of unit monosaccharides due to oxygen-derived free radicals, followed by secondary hydrolytic cleavage of the resulting unstable glycosidic substituents.

Acetylglucosamine↗