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PubMed1990

Structure and oxidation-reduction behavior of 1-deaza-FMN flavodoxins: modulation of redox potentials in flavodoxins.

Flavodoxins from Clostridium beijerinckii and from Megasphaera elsdenii with 1-carba-1-deaza-FMN substituted for FMN have been used to study flavin-protein interactions in flavodoxins. The oxidized 1-deaza analogue of FMN binds to apoflavodoxins from M. elsdenii and C. beijerinckii (a.k.a. Clostridium MP) with association constants (Ka) of 1.0 x 10(7) M-1 and 3.1 x 10(6) M-1, values about 10(2) less than the corresponding Ka values for FMN. X-ray structure analysis of oxidized 1-deaza-FMN flavodoxin from C. beijerinckii at 2.5-A resolution shows that the analogue binds with the flavin atoms in the same locations as their equivalents in FMN but that the protein moves in the vicinity of Gly 89 to accommodate the 1-CH group, undergoing displacements which increase the distance between position 1 of the flavin ring and the main-chain atoms of Gly 89 and move the peptide hydrogen of Gly 89 by about 0.6 A. The X-ray analysis implies that protonation of normal flavin at N(1), as would occur in formation of the neutral fully reduced species, would result in a similar structural perturbation. The oxidation-reduction potentials of 1-deaza-FMN flavodoxin from M. elsdenii have been determined in the pH range 4.5-9.2. The oxidized/semiquinone equilibrium (E'0 = -160 mV at pH 7.0) displays a pH dependence of -60 mV per pH unit; the semiquinone/reduced equilibrium (E'0 = -400 mV at pH 7.0) displays a pH dependence of -60 mV per pH unit at low pH and is pH independent at high pH, with a redox-linked pK of 7.4. Spectral changes of fully reduced 1-deaza-FMN flavodoxin with pH suggest that this latter pK corresponds to protonation of the flavin ring system (the pK of free reduced 1-deaza-FMN is 5.6 [Spencer, R., Fisher, J., & Walsh, C. (1977) Biochemistry 16, 3586-3593]. The pK of reduced 1-deaza-FMN flavodoxin provides an estimate of the electrostatic interaction between the protein and the bound prosthetic group; the free energy of binding neutral reduced 1-deaza-FMN is more negative than that for binding the anionic reduced 1-deaza-FMN by 2.4 kcal.(ABSTRACT TRUNCATED AT 250 WORDS)

Clostridium↗
PubMed1975

Requirement of low oxidation-reduction potential for photosynthesis in a blue-green alga (Phormidium sp.).

Photosynthesis in a Phormidium species which forms dense conical-shaped structures in thermal springs is strongly inhibited by aeration but is stimulated by sulfide and other agents (cysteine, thioglycolate, sulfite) which lower the oxidation-reduction potential. The compact structures which this alga forms in nature may restrict oxygen penetration from the enviroment so that the anaerobic or microaerophilic conditions necessary ofr photosynthesis can develop. The alga may be defective in a regulatory mechanism that controls the reoxidation of reduced pyridine nucleotides formed during photosynthesis. It is suggested that other mat-forming and benthic blue-green algae may also prefer anaerobib conditions for growth and photosynthesis.

Anaerobiosis↗
PubMed1986

Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties.

The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex. With the exception of 3'-NADP+, only adenosine nucleotides with a 2'-adenosyl phosphate bound to Fd-NADP+ reductase. Kd values increased in the order: 2',5'-ADP greater than 2',5'-ATP ribose greater than NADP+ greater than 2'-AMP greater than 3'-NADP+. No evidence was found for binding of NAD, NMN, or 5'-ADP. Thus the 2'-adenosylphosphate controls specificity in substrate binding, as well as specificity in enzyme activity. The low affinity of Fd-NADP+ reductase for 2'-AMP suggests that the phosphate(s) of the pyrophosphate bridge of NADP+ may also contribute significantly to binding energy. Fd-NADP+ reductase was found to form a high-affinity two-electron reduced complex (FNR.NADPH) with a NADPH; complex formation was associated with appearance of long-wavelength charge-transfer bands. Kd of FNR.NADPH complex was about 6% the Kd of oxidized FNR.NADP+ complex. As predicted by the lower Kd, the Em for reduction of FNR.NADP+ complex to the charge-transfer complex was about 40 mV more positive than the potential of the NADP+/NADPH couple. Rapid kinetic studies supported description of the charge-transfer complex as primarily oxidized FNR.NADPH. Thus, complex formation helps drive electron transfer from the flavoprotein to NADP+.

Adenine Nucleotides↗
PubMed1992

Chemical change involved in the oxidative-reductive depolymerization of heparin.

A solution of hog intestinal heparin (average M(r) 12,000, anti-clotting activity 168 USP units/mg) in 0.2 M phosphate buffer (pH 7.2), was incubated in the presence of Fe2+ for 20 h at 50 degrees under an O2 atmosphere to yield oxidative-reductively depolymerized heparin (ORD heparin, average M(r) 3,000, anti-clotting activity 34 USP units/mg). Chemical analysis of the ORD heparin showed a 22, 26, and 14% loss of hexosamine, uronic acid, and N-acetyl group, respectively, but no remarkable loss of both total and N-sulfate groups. 1H and 13C NMR spectroscopic analysis indicated no decrease in the amount of L-iduronic acid 2-sulfate, but a marked loss of nonsulfated uronic acid (73 and 39% loss of D-glucuronic acid and L-iduronic acids, respectively, the sum of which corresponds to the chemically determined loss of total uronic acid). The results indicated that the ORD reaction of heparin proceeds essentially by destruction of monosaccharide units, except L-iduronic acid 2-sulfate residues, due to oxygen-derived free radicals, followed by secondary hydrolytic cleavage of the resulting unstable residues.

Carbohydrates↗
PubMed2004

Escherichia coli proton-translocating F0F1-ATP synthase and its association with solute secondary transporters and/or enzymes of anaerobic oxidation-reduction under fermentation.

The Escherichia coli proton-translocating F0F1-ATP synthase has a priority in H+ circulation through the membrane in maintaining proton-motive force in the context of ATP synthesis and hydrolysis. Recent advances in the study of this complex under fermentative growth have led to hypothesis that, in the absence of oxidative phosphorylation, F0F1 is implicated as an essential part of H+ movement and ATP hydrolysis, associated with solute secondary transporters and/or enzymes of anaerobic oxidation-reduction. These associations can result from a protein-protein interaction by dithiol-disulfide interchange. In such associations F0F1 has novel functions in bacterial cell physiology.

Aerobiosis↗
PubMedDate not supplied

Oxidation-reduction potential changes in aeration tanks and microprofiles of activated sludge floc in medium- and low-strength wastewaters.

Real-time control of aeration tank operation is key to high-efficiency pollutant removal and energy savings. One of the aims of this study was to examine the potential for using redox potential (oxidation-reduction potential [ORP]) to indicate wastewater quality online in aeration tanks treating medium (chemical oxygen demand [COD] of 70 to 150 mg/L) and low (COD of 15 to 30 mg/L) pollutant-concentration wastewaters. The field-scale data provide a good relationship between ORP values and nutrient removal along the length of the aeration tanks. The ORP values increased dramatically as organic matter was removed along the aeration tanks, indicating the improvement of the bulk liquor redox status. Dissolved oxygen higher than 1.0 mg/L was necessary for good biodegradation and improvement of the liquid redox status. Nitrification occurred at higher ORP values (380 to 420 mV) than was the case for organic substrate oxidation (250 to 300 mV). The microprofiles obtained from microelectrode measurements substantiate the heterogeneity of the microbial processes inside activated sludge flocs. Because of microbial oxygen utilization, the aerobic region in the activated sludge floc was limited to the top layer (0.1 to 0.2 mm) of the activated sludge aggregate present in medium-strength wastewater, with an anoxic zone dominating inside the flocs. When dissolved oxygen in the bulk water was higher than 4.0 mg/L, the anoxic zone inside the floc disappeared. At low wastewater pollutant concentrations, the ORP and dissolved oxygen inside the activated sludge aggregates were higher than those from medium-strength wastewater. The prospect of using ORP as an online control approach for aeration tank operation and the potential reasons for activated sludge floc size varying with pollutant strengths are also discussed.

Air Movements↗
PubMed2004

The appearance and disappearance of antiphospholipid autoantibodies subsequent to oxidation--reduction reactions.

The mechanisms that cause the appearance of autoantibodies are not understood. Compared to normal antibody production, factors responsible for autoantibody synthesis are more complex; they are thought to disrupt the normal mechanisms proposed to eliminate or down-regulate self-antibodies or to interfere with anti-self-receptor editing. Data presented show that autoantibodies exist in the blood of all normal individuals. The autoantibodies appear after simple oxidation-reduction (redox) reactions and react by ELISA, immunofluorescence, flow cytometry, Western blots, and in lupus anticoagulant (LA) assays. Antiphospholipid antibody (aPL) specificities detected after redox are cardiolipin (aCL), antiphosphatidylserine (aPS), antiphosphatidylethanolamine (aPE), antiphosphatidylcholine (aPC), and LA. These antibody activities were confirmed in several outside laboratories. The aPL isotypes detected in ELISA are plasma protein-dependent and include IgG, IgA, and IgM. Oxidizing agents tested to date include hemin, KMnO4, and NaIO4. Furthermore, aPL appear after exposure to direct current (DC)-mediated electromotive force. Alternating current (AC) is ineffective. Commercial IvIg preparations, also a source of IgG autoantibodies, provide a less complex milieu than plasma or serum for studying the biology of aPL redox-mediated mechanisms. Inhibition of hemin-mediated IvIg aPL conversion can be achieved by the addition of antioxidants, e.g., ascorbic acid, hemopexin, apotransferrin, and by addition of normal plasma or serum. Remarkably, the aPL specificities in the blood of autoimmunity patients disappear subsequent to application of redox reactions. These data document the hitherto unknown existence of redox-reactive autoantibodies in all normal individuals. The evolutionary persistence of these redox-sensitive antibodies raises interesting possibilities about their potentially beneficial role in immunological homeostasis.

Antibodies, Antiphospholipid↗
PubMed2006

Age-related changes in activity of enzymes catalyzing oxidation-reduction of endogenous aldehydes in the liver of rats during immobilization stress.

Activities of aldehyde dehydrogenase and aldehyde reductase in the liver 1.5-, 12-, and 24-month-old rats were measured after 30-min immobilization. Changes in activities of aldehyde dehydrogenase and aldehyde reductase in the liver after immobilization stress depended on animal age. These shifts lead to a strain in endogenous aldehyde utilization in the aldehyde reductase reaction in 1.5-month-old animals and inhibition of utilization of these metabolites in oxidation-reduction reactions in 24-month-old rats.

Age Factors↗
PubMed1993

[Cytochemical definition of oxidation-reduction enzyme activity peripheral blood lymphocytes in patients with thyrotoxic goiter].

In patients with thyrotoxic goiter (TTG), a significant decrease in the activity of alpha-glycerophosphate-dehydrogenase and adenosinetriphosphatase of the peripheric blood lymphocytes was revealed. The lowest indices were noted in patients with a severe form of TTG, who underwent strumectomy. After conservative and operative treatment of TTG, a tendency for normalization of the enzyme activity was observed. Study of changes in the activity of the oxidation-reduction lymphocytic enzymes in dynamics permits to assess the severity of the course of TTG and to control and predict the effectiveness of treatment as well.

Adenosine Triphosphatases↗
PubMed2003

Controlling a combined lagoon/reed bed system using the oxidation-reduction potential (ORP).

Lagoon systems achieve good and stable effluent data in regard to organic pollutants, but they charge the receiving waters with relatively high ammonium loads. Therefore an existing lagoon-plant was extended by a vertical flow reed-bed for the special purpose of nitrification. This paper presents the efficiency of the combination plant as well as the possibility to monitor and control the reed-bed operation by the oxidation-reduction potential (ORP). The results show that the combination plant achieved excellent purification results, the average efficiency degrees were 97% for COD, 77% for N(total) and 94% for the TKN elimination. The ORP in the effluent of the reed bed showed a clear dependence in its characteristic course and its absolute values on the current nitrification performance, the oxygen supply and the hydraulic behaviour of the reed bed. Therefore the ORP is a very good indicator for the state of the reed bed, which ultimately results from the accumulation of a large number of different influencing parameters. As the preservation of aerobic conditions in the reed bed is the crucial prerequisite for a high nitrification performance and for the avoidance of clogging, the ORP thus offers the possibility of immediate operation control.

Ecosystem↗
PubMed1982

Quantitative histochemical resolution of the oxidation-reduction and phosphate potentials within the simple hepatic acinus.

Glycerin-3-P, commonly known as alpha-glycerophosphate and dihydroxyacetone phosphate (DHAP) were measured in well defined microscopic samples of the simple liver acinus allowing a comparison of the glycerin-3-P/dihydroxyacetone-P-ratios of Zones 1 and 3 as a measure of the free NAD+/NADH ratio. The ATP/ADP X Pi quotients were determined in these same microscopic areas of the liver acinus as a measure of the phosphate potential. Brief ischemia was used to disturb the system. The results indicate that the oxidation-reduction and phosphate potentials are uniform throughout the entire liver lobule.

Animals↗
PubMed1990

Effects of molecular oxygen, oxidation-reduction potential, and antioxidants upon in vitro replication of Treponema pallidum subsp. pallidum.

The effects of various concentrations of dithiothreitol, molecular oxygen, and several antioxidants upon the in vitro replication of Treponema pallidum were studied. The optimal dithiothreitol concentration was between 0.65 and 1.62 mM, and the optimum oxygen concentration was 3.0% +/- 0.5% in both the presence and absence of additional antioxidants. It was discovered that the reduced sulfhydryl concentration and the oxidation-reduction potential of the medium were stabilized after 5 days. The water-soluble antioxidants cobalt chloride, cocarboxylase, mannitol, and histidine were individually tested for their ability to increase treponemal growth in vitro. The optimum concentrations for these antioxidants were 21 nM, 4.3 nM, 0.55 mM, and 0.23 mM, respectively. When combined at these concentrations, the mixture of antioxidants stimulated the in vitro replication of T. pallidum. The number of treponemes in cultures with the antioxidants averaged a 59-fold increase, compared with a 43-fold increase in cultures lacking the antioxidants. It was further demonstrated that histidine and mannitol were the most critical components of this mixture. Catalase and superoxide dismutase were investigated for their ability to promote the growth and maintain viability of T. pallidum in tissue culture. The optimum concentrations for these enzymes were 10,000 U/liter and 25,000 U/liter, respectively. When these enzymes and the above antioxidants were combined and added to a chemically reduced modified Eagle medium, the treponemes increased an average of 70-fold, compared with an average of 35-fold in cultures lacking them. Furthermore, this medium, T. pallidum culture medium, supported the replication of T. pallidum at oxygen concentrations from 5 to 7% with little loss in yield or viability. The lipid-soluble antioxidants vitamin A and vitamin E acetate were also shown to enhance the in vitro growth of T. pallidum in this medium.

Antioxidants↗
PubMed1994

Site-directed mutagenesis of tyrosine-98 in the flavodoxin from Desulfovibrio vulgaris (Hildenborough): regulation of oxidation-reduction properties of the bound FMN cofactor by aromatic, solvent, and electrostatic interactions.

The contributions made by tyrosine-98 in establishing the redox properties of the flavodoxin from Desulfovibrio vulgaris were investigated by substituting a number of amino acids at this position using site-directed mutagenesis. Tyr98, which makes extensive van der Waals contacts with the isoalloxazine ring of the flavin mononucleotide cofactor, is often found in the cofactor binding site of flavodoxins and related flavoproteins. Solution studies suggest that tyrosine may assist in the stabilization of the neutral flavin semiquinone through preferential complex formation relative to the other oxidation states. In this study, the midpoint potentials of the oxidized/semiquinone couple of the Y98W and Y98F mutants were found to be very similar to the wild-type flavodoxin. However, significantly more negative midpoint potentials (by 25-60 mV) were observed in the Y98A, Y98H, and Y98R mutants. These results imply that it is the general apolar environment provided by the aromatic amino acids rather than preferential affinities suggested by solution studies that is at least partially responsible for the thermodynamic stabilization of the neutral flavin semiquinone in this flavodoxin. The midpoint potential of the semiquinone/hydroquinone couple is profoundly dependent on the properties of the amino acid at this position. Compared to phenylalanine, the more electron-rich aromatic side chains of tryptophan and tyrosine decrease the midpoint potential of this couple by 30-40 mV. Greater solvent exposure of the isoalloxazine ring in the Y98A mutant increases the midpoint potential by 140 mV relative to wild type. The positively charged amino acids increase the midpoint potential of this couple by > 180 mV, most probably through favorable electrostatic interactions with the flavin hydroquinone anion. These observations strongly support the proposition that the functional role of the electron-rich, apolar aromatic amino acid residues adjacent to the flavin isoalloxazine ring is to substantially destabilize the flavin hydroquinone anion, resulting in the very low oxidation-reduction potentials for the semiquinone/hydroquinone couple that typify the flavodoxin family.

Binding Sites↗
PubMed1981

Copper(I) . bleomycin. A structurally unique oxidation-reduction active complex.

Cu(I) and Cu(II) form stable 1:1 complexes with bleomycin (BLM). The affinity of both metals for the drug is greater than that of Fe(II). Cu(I) . BLM A2 binds to calf thymus DNA with about the same affinity as Fe(II) . BLM, as judged by DNA-induced fluorescence quenching of the bithiazole moiety of BLM. Based on 1H NMR and potentiometric titration data, the Cu(I) complexes of BLM are shown to have geometries very different than those of other BLM . metal(II) complexes studied thus far. As Cu(I) . BLM is oxidation-reduction active, its geometry is of importance in defining the structural requirements for BLM activity.

Animals↗