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PubMed2000

Lack of production of electron-shuttling compounds or solubilization of Fe(III) during reduction of insoluble Fe(III) oxide by Geobacter metallireducens.

Studies with the dissimilatory Fe(III)-reducing microorganism Geobacter metallireducens demonstrated that the common technique of separating Fe(III)-reducing microorganisms and Fe(III) oxides with semipermeable membranes in order to determine whether the Fe(III) reducers release electron-shuttling compounds and/or Fe(III) chelators is invalid. This raised doubts about the mechanisms for Fe(III) oxide reduction by this organism. However, several experimental approaches indicated that G. metallireducens does not release electron-shuttling compounds and does not significantly solubilize Fe(III) during Fe(III) oxide reduction. These results suggest that G. metallireducens directly reduces insoluble Fe(III) oxide.

Deltaproteobacteria↗
PubMed2026

Integrated photoelectrocatalytic reduction and oxidation processes to achieve efficient degradation of fluoxetine in pharmaceutical wastewater.

Fluorinated organic compounds have been frequently detected in aquatic environments, with the widespread use of fluorinated drugs. The existing processes of urban sewage treatment plants are difficult to completely remove these pollutants containing the persistent C-F bonds. In this work, an integrated system of UV-activated sulfite and UV-assisted electrochemical oxidation was innovatively constructed for efficient degradation of fluoxetine. For the UV-activated sulfite unit system, when the sulfite dosage was 0.5 mmol/L and the initial pH was about 10, the defluorination efficiency of 5 mg/L fluoxetine wastewater under nitrogen atmosphere was about 98 %. Subsequently, the UV-assisted electrochemical oxidation unit system was employed to treat the reduced wastewater mentioned above. When the sodium chloride dosage was 25 mmol/L, the initial pH was about 5, and the current density was 30 mA/cm2, the total organic carbon (TOC) removal of the wastewater arrived at 65 %. Active species capture experiments and ESR tests confirmed that hydrated electrons, hydroxyl, and chlorine radicals were the main components for the efficient degradation of fluoxetine. According to the analysis of Fukui function and HPLC-MS, the degradation pathway of pollutants was proposed including defluorination and mineralization. Meanwhile, the toxicity of intermediates was predicted using the ECOSAR program. In addition, the verification test of actual wastewater treatment indicated that the defluorination and TOC removal efficiency of fluorouracil by the integrated system were similar to those for fluoxetine. This work provided a new approach for the efficient degradation of fluorinated organic pollutants in pharmaceutical wastewater.

Fluoxetine↗
PubMed2002

Oxysulfide Sm(2)Ti(2)S(2)O(5) as a stable photocatalyst for water oxidation and reduction under visible light irradiation (lambda < or = 650 nm).

A Ti-based oxysulfide, Sm(2)Ti(2)S(2)O(5), was studied as a visible light-driven photocatalyst. Under visible light (440 nm < or = lambda < or = 650 nm) irradiation, Sm(2)Ti(2)S(2)O(5) with a band gap of approximately 2 eV evolved H(2) or O(2) from aqueous solutions containing a sacrificial electron donor (Na(2)S-Na(2)SO(3) or methanol) or acceptor (Ag(+)) without any noticeable degradation. This oxysulfide is, therefore, a stable photocatalyst with strong reduction and oxidation abilities under visible-light irradiation. The electronic band structure of Sm(2)Ti(2)S(2)O(5) was calculated using the plane-wave-based density functional theory (DFT) program. It was elucidated that the S3p orbitals constitute the upper part of the valence band and these orbitals make an essential contribution to the small band gap energy. The conduction and valence bands' positions of Sm(2)Ti(2)S(2)O(5) were also determined by electrochemical measurements. It indicated that conduction and valence bands were found to have satisfactory potentials for the reduction of H(+) to H(2) and the oxidation of H(2)O to O(2) at pH = 8. This is consistent with the results of the photocatalytic reactions.

Journal Article↗
PubMed1980

Kinetics of oxidation and reduction of high-potential iron-sulfur proteins with nonphysiological reactants.

We have investigated the kinetic and equilibrium oxidation-reduction properties of HIPIP's from four sources: Chromatium vinosum, Thiocapsa pfennigii, Rhodopseudomonas gelatinosa, and a paracoccus sp. These studies focused on the interaction of the various HIPIP's and the iron hexacyanides as a function of ionic strength, pH, and temperature. On the basis of the kinetic and equilibrium data obtained and the known structrual properties of the various HIPIP's a number of conclusions concerning the mechanism of electron transfer by HIPIP can be inferred. (1) The oxidation and reduction of HIPIP by the iron hexacyanides show no kinetic complexity due to heterogeneity or changes in rate-limiting step. (2) The kinetic and equilibrium studies (oxidation-reduction potential) are in good agreement, although a rapid binding equilibrium between HIPIP and the iron hexacyanides is possible. (3) The kinetics of oxidation and reduction of the various HIPIP's studied do not correlate with their oxidation-reduction potentials. (4) The electrostatic interactions between a particular HIPIP and the iron hexacyanides appear to be influenced by the charge on the iron-sulfur cluster with specific amino acid side chains playing a significant but limited role in the interactions leading to electron transfer. (5) The iron-sulfur cluster charge is apparently distributed on the surface of the HIPIP molecule through a network of hydrogen bonds. (6) On the basis of an analysis of the known primary and tertiary structure of the HIPIP's studied, it is concluded that peptide backbone carbonyls and amino acid side chains for the amino acid sequence positions 46-49, 63-65, 78-82, 31-34, and 16-17 define the interaction site of HIPIP and the iron hexacyanides irrespective of the HIPIP source. This is a structural region at which the iron-sulfur cluster is near to the protein surface and in this respect resembles the active site in mitochondrial cytochrome c.

Amino Acid Sequence↗
PubMed1998

Ceruloplasmin copper induces oxidant damage by a redox process utilizing cell-derived superoxide as reductant.

Oxidative damage by transition metals bound to proteins may be an important pathogenic mechanism. Ceruloplasmin (Cp) is a Cu-containing plasma protein thought to be involved in oxidative modification of lipoproteins. We have previously shown that Cp increased cell-mediated low-density lipoprotein (LDL) oxidation by a process requiring cell-derived superoxide, but the underlying chemical mechanism(s) is (are) unknown. We now show that superoxide reduction of Cp Cu is a critical reaction in cellular LDL oxidation. By bathocuproine disulfonate (BCS) binding and by superoxide utilization, we showed that exogenous superoxide reduces a single Cp Cu atom, the same Cu required for LDL oxidation. The Cu atom remained bound to Cp during the redox cycle. Three avenues of evidence showed that vascular cells reduce Cp Cu by a superoxide-dependent process. The 2-fold higher rate of Cp Cu reduction by smooth muscle cells (SMC) compared to endothelial cells (EC) was consistent with their relative rates of superoxide release. Furthermore, Cp Cu reduction by cells was blocked by Cu,Zn superoxide dismutase (SOD1). Finally, the level of superoxide produced by EC and SMC was sufficient to cause the amount of Cu reduction observed. An important role of Cp Cu reduction in LDL oxidation was suggested by results showing that SOD1 inhibited Cp Cu reduction and LDL oxidation by SMC with equal potency, while tumor necrosis factor-alpha stimulated both processes. In summary, these results show that superoxide is a critical cellular reductant of divalent transition metals involved in oxidation, and that protein-bound Cu is a substrate for this reaction. The role of these mechanisms in oxidative processes in vivo has yet to be defined.

Animals↗
PubMed1997

Measurement of Electron Transfer Rates between Adsorbed Azurin and a Gold Electrode Modified with a Hexanethiol Layer

In this work we report the application of electroreflectance (ER) spectroscopy for the study of the redox reaction of the nonheme protein azurin. Azurin was irreversibly adsorbed on a polycrystalline gold surface modified with a hexanethiol layer. Surface-enhanced resonant Raman spectroscopy (SERRS) demonstrated that the immobilized azurin's copper site remained intact upon adsorption and that it underwent reversible reduction-oxidation. Cyclic voltammetry (CV) data showed that the peak current of the oxidation (or reduction) wave depended linearly on the sweep rate as appropriate for an immobilized species. The formal potential of the adsorbed azurin was 95 &plusmn; 8 mV vs Ag/AgCl electrode, nearly identical to the earlier observed value of the native azurin in solution. All measurements were analyzed in the context of Marcus theory of electron transfer. The separation of the reduction-oxidation peaks in the CV data gave an estimate of the electron transfer (ET) rate in the range from 4 to 12 s-1. ER, with light of wavelength of 640 nm, yielded a strong signal at the same potential as the midpotential determined in CV. The frequency dependence of the ER response was consistent with an ET rate of 150 to 200 s-1. Electrochemical impedance measurements indicated an ET rate of the order of 300 s-1. The disparity between the ET rates measured with CV and ER suggests that ET may not be a single-step process. The results also point to the importance of hydrophobic interactions in adsorption and redox transformations of azurin. Copyright 1997Academic Press

Journal Article↗
PubMed1994

The effects of thiol reduction and oxidation on the inhibition of NMDA-stimulated neurotransmitter release by ethanol.

The N-methyl-D-aspartate (NMDA) receptor is sensitive to inhibition by pharmacologically relevant concentrations of ethanol and may be an important target for the actions of ethanol in the brain. The mechanisms responsible for ethanol's action are unknown but may involve perturbation of one of the multiple regulatory sites that have been identified on the receptor. Previous studies have shown that thiol reducing and oxidizing agents selectively after the activity of the NMDA receptor via a redox modulatory site. In this study, these agents were tested for their ability to modify the inhibitory actions of ethanol on NMDA-stimulated neurotransmitter release from rat brain slices and the potentiation of NMDA-stimulated release by the glycine agonist D-serine. Treatment of hippocampal slices with the thiol reducing agent dithiothreitol (DTT) significantly potentiated (> 2-fold) the NMDA-stimulated release of tritiated norepinephrine ([3H]NE) from rat hippocampal slices. Slices treated with the thiol oxidizing agent dithionitrobenzoic acid (DTNB) had slightly lower (10-15%) levels of NMDA-stimulated neurotransmitter release. Ethanol (25-200 mM) dose-dependently inhibited the NMDA-stimulated release of [3H]NE from control slices with a calculated IC50 value of 73.1 mM. The inhibitory potency for ethanol was increased following DTNB treatment (IC50 of 40.9 mM) while DTT treatment slightly reduced ethanol's potency (IC50 of 85.6 mM). The ability of D-serine to augment NMDA-stimulated neurotransmitter release was tested in the presence and absence of ethanol following treatment of slices with either DTT or DTNB to examine any potential interaction between these modulatory sites.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1998

Reduction of oxidation during the preparation of DNA and analysis of 8-hydroxy-2'-deoxyguanosine.

The promutagenic base 8-hydroxy-2'-deoxyguanosine (8-OH-dG) in DNA is known to be formed from oxygen radical attack on 2'-deoxyguanosine (dG) as a result of oxidative stress. Formation of 8-OH-dG from dG during workup is strongly dependent on temperature and transition metals and is mediated by oxygen radicals. The 8-OH-dG formation at temperatures between 0 and 140 degrees C for 1.5 h in an "ultrapure" solution followed a third-order equation. Fe2+ in the nM range mediated the formation of 8-OH-dG from dG without addition of H2O2. Fe3+, Cu+, and Cu2+ were shown to have weaker oxidative effects in comparison to Fe2+. The pH (5.0-9.0) had a very limited effect on 8-OH-dG formation. Acid phosphatase, which contains iron at its active site, caused the formation of 8-OH-dG, whereas alkaline phosphatase did not. Phenol was not found to be oxidative. Fe2+-catalyzed formation of 8-OH-dG was completely blocked by the nitroxide 2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO), whereas DMSO, mannitol, and DMPO had a significantly weaker protecting effect. Catalase cleaved the dG molecule and was not suitable for use. A simple, fast, and inexpensive method for 8-OH-dG workup and analysis was developed, and the background level seen in liver from 13-week-old male Sprague-Dawley rat was 0.23 +/- 0.020 8-OH-dG/10(5) dG, which is up to 200 times lower than reported values from some other methods and up to 26 times lower when compared to other reports using HPLC-EC methods. In summary, the TEMPO method reduces oxidation of dG to 8-OH-dG during workup by (1) using chemicals low in transition metals, (2) using a cold workup procedure, (3) limiting the incubation time, and (4) using the nitroxide TEMPO in all steps.

8-Hydroxy-2'-Deoxyguanosine↗
PubMed1981

Enzymatic reduction of oxidized alpha-1-proteinase inhibitor restores biological activity.

The major serum inhibitor of proteolytic activity, alpha-1-proteinase inhibitor (alpha-1-PI), (or alpha-1-antitrypsin) can be readily inactivated by oxidation [Carp, H. & Janoff, A. (1978) Am. Rev. Resp. Dis. 118, 617-621]. This inactivation appears to be due to the oxidation of a critical methionine(s) in alpha-1-PI that is required for the inhibition of elastase activity. An enzyme from Escherichia coli that reduces methionine sulfoxide residues in protein [Brot, N., Weissbach, L., Werth, J. & Weissbach, H. (1981) Proc. Natl. Acad. Sci. USA 78, 2155-2158] can restore the biological inhibitory activity of canine oxidized alpha-1-PI.

Animals↗