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At least 19 recordsLinked to original sources
PubMed1984

Graphical analysis of interactions between oxidation-reduction sites in two site oxidation-reduction proteins.

Many enzymes that catalyze electron-transfer reaction contain multiple oxidation-reduction centers (sites). The oxidation-reduction potential of one site as well as the kinetics of electron transfer through this site may be altered by the state of reduction of a neighboring site. Oxidation-reduction site interactions may be mechanistically important and quantitation of site interactions would aid the interpretation of thermodynamic data and possibly kinetic data. A graphical means to detect and quantitate interactions between oxidation-reduction sites from oxidation-reduction equilibrium data (type A + B in equilibrium C + D) is described and has its roots in the Scatchard analysis of ligand binding equilibria (type A + B in equilibrium C). Oxidation-reduction sites often have distinct physical properties allowing the titration behavior of specific sites to be monitored. Equilibrium measurements on specific sites of a two site protein allow a further analysis of the data which can be combined with the oxidation-reduction Scatchard analysis to solve for all four specific site equilibrium constants. Ligand binding systems can usually measure only total site binding and simplifying assumptions of identical sites or noninteracting sites are required to solve for the site specific equilibrium constants. Thus, specific site equilibrium measurements offer a distinct advantage over total site measurements. The principles of the method are illustrated by applying the graphical analysis to the two site protein, thioredoxin reductase, which contains an oxidation-reduction active site disulfide in addition to FAD. The specific site oxidation-reduction midpoint potentials (Em) of the FAD and disulfide couples of thioredoxin reductase at pH 6.0, 12 degrees C, were found to be FAD/FADH2-enzyme-(S)2 = -0.183 V, FAD/FADH2-enzyme-(SH)2 = -0.199 V, (FAD)-enzyme-(S)2/(SH)2 = -0.202 V, and (FADH2)-enzyme-(S)2/(SH)2 = -0.218 V. Hence, at pH 6.0, the FAD and disulfide sites of thioredoxin reductase have Em values that differ by approximately 0.019 V and have a negative interaction of about 0.016 V.

Binding Sites↗
PubMed2000

[Oxidation-reduction processes in patients with recurring nephrolithiasis complicated with chronic pyelonephritis and urostasis during combined treatment].

Results of study into the condition of reduction-oxidation processes, in particular of those associated with generation of the superoxide radical, are submitted together with those of determination of levels of inorganic phosphate which is known to be an important indicator of the tissue bioenergy potential, in 112 patients presenting with a recurring form of nephrolithiasis exposed to a multiple-modality treatment that included conventional antiinflammatory and antibacterial therapy plus "open" and endourological operations on kidneys and ureters. The multiple-modality treatment of the main group patients was supplemented with phlogenzyme, a drug of II generation systemic enzymotherapy. An enhanced generation of superoxide radical was recordable having developed in the wake of a steady increase in the activity of xanthinoxidase. The authors have come to the conclusion that the conducted therapeutic intervention, especially as part of systemic enzyme therapy, results in decline of activity of the xanthine oxidation processes and brings about a change in the blood:urine inorganic phosphate concentrations ratio.

Chronic Disease↗
PubMed2002

Biological iron oxidation-reduction and the effects on sulfur oxidation-reduction, denitrification and poly-P accumulation in an anaerobic-oxic activated sludge.

Iron oxidation and reduction were examined using the activated sludge from a municipal plant. Iron contents of the activated sludge were 1-2%. Iron oxidation rates were correlated with the initial iron concentrations. Iron reducing rates could be described by the Monod equation. The effects of iron reducing bacteria on sulfate reduction, denitrification and poly-P accumulation were examined. Iron reduction suppressed sulfate reduction by competing with hydrogen produced from protein. Denitrification was outcompeted with iron reduction and sulfate reduction. These phenomena could be explained thermodynamically. Poly-P accumulation was also suppressed by denitrification. The activity of iron reduction was relatively high.

Bacteria, Anaerobic↗
PubMed1992

Effect of acetylene on nitrous oxide reduction and sulfide oxidation in batch and gradient cultures of Thiobacillus denitrificans.

Anaerobic enrichment cultures with H2S and N2O as substrates which were inoculated with a biofilm sample showed rapid growth and gas formation after 2 to 3 days at 27 degrees C. By using the deep-agar dilution technique, a pure culture was obtained. The strain was tentatively identified as Thiobacillus denitrificans. The isolate was used for batch and gradient culture studies under denitrifying conditions, oxidizing H2S with concomitant reduction of N2O to N2. In batch culture, oxidation of H2S was stepwise, with transient accumulation of elemental sulfur; the final oxidation product was SO4(2-). In gradient culture, there was no notable accumulation of elemental sulfur and microsensor measurements of H2S and N2O showed that H2S was oxidized directly to SO4(2-). In the presence of C2H2, however, oxidation of H2S stopped at the level of elemental sulfur and no SO4(2-) was produced in either batch or gradient cultures. This is a hitherto unknown inhibitory effect of C2H2. The inhibition is suggested to occur at the level of sulfite reductase, which catalyzes the oxidation of elemental sulfur to SO3(2-) in T. denitrificans. However, reduction of N2O in this strain was, surprisingly, not affected by C2H2. The isolate is the first chemolithoautotrophic organism shown to reduce N2O in the presence of C2H2. Denitrification in natural ecosystems is often quantified as N2O accumulation after C2H2 addition. However, the presence of large numbers of similar organisms with C2H2-insensitive N2O reduction could lead to underestimation of in situ rates.

Acetylene↗
PubMed1984

Measurement of the oxidation-reduction potentials for one-electron and two-electron reduction of electron-transfer flavoprotein from pig liver.

Potentiometric titrations of pig liver electron-transfer flavoprotein (ETF) were performed at pH 7.5 and 4 degrees C, both in the reductive and oxidative directions. Reduction of ETF to the hydroquinone form required a total of two reducing equivalents/mol of ETF with the formation of sub-stoichiometric amounts of anionic semiquinone as an intermediate. The oxidation-reduction potentials for the two one-electron couples, oxidized ETF/ETF semiquinone and ETF semiquinone/fully reduced ETF, are +4 mV and -50 mV respectively. The overall midpoint potential for the two-electron couple (oxidized ETF/fully reduced ETF) is -23 mV.

Animals↗