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PubMed1984

On the mechanism of action of cytochrome P-450. Oxidation and reduction of the ferrous dioxygen complex of liver microsomal cytochrome P-450 by cytochrome b5.

The effects of cytochrome b5 on the decay of the ferrous dioxygen complexes of P-450LM2 and P-450LM4 from rabbit liver microsomes were studied by stopped-flow spectrophotometry. The P-450 (FeIIO2) complexes accept an electron from reduced cytochrome b5 and, in a reaction not previously described, donate an electron to oxidized cytochrome b5 to give ferric P-450. A comparison with the electron-transferring properties of ferrous P-450 under anaerobic conditions allowed determination of the limiting steps of the two reactions involving the oxygenated complex. The rate of decay of the dioxygen complex was increased in all cases with b5 present; however, with oxidized b5 a large increase in the rate was observed with P-450 isozyme 4 but not with isozyme 2, whereas the opposite situation was found when reduced b5 was used. The reactions between b5 and ferrous dioxygen P-450 were not at thermodynamic equilibrium under the conditions employed. From the results obtained, a model is proposed in which the ferrous dioxygen complex decomposes rapidly into another species differing from ferric P-450 in its spectral properties and from the starting complex in its electron-transferring properties. A scheme is presented to indicate how competition among spontaneous decay, cytochrome b5 oxidation, and cytochrome b5 reduction by the ferrous O2 complex may influence substrate hydroxylation.

Aerobiosis↗
PubMed2002

Antioxidant and prooxidant mechanisms in the regulation of redox(y)-sensitive transcription factors.

A progressive rise of oxidative stress due to the altered reduction-oxidation (redox) homeostasis appears to be one of the hallmarks of the processes that regulate gene transcription in physiology and pathophysiology. Reactive oxygen (ROS) and nitrogen (RNS) species serve as signaling messengers for the evolution and perpetuation of the inflammatory process that is often associated with the condition of oxidative stress, which involves genetic regulation. Changes in the pattern of gene expression through ROS/RNS-sensitive regulatory transcription factors are crucial components of the machinery that determines cellular responses to oxidative/redox conditions. Transcription factors that are directly influenced by reactive species and pro-inflammatory signals include nuclear factor-kappaB (NF-kappaB) and hypoxia-inducible factor-1alpha (HIF-1alpha). Here, I describe the basic components of the intracellular oxidative/redox control machinery and its crucial regulation of oxygen- and redox-sensitive transcription factors such as NF-kappaB and HIF-1alpha.

Animals↗
PubMed2006

A hollow tetrahedral cage of hexadecagold dianion provides a robust backbone for a tuneable sub-nanometer oxidation and reduction agent via endohedral doping.

We show, via density functional theory calculations, that dianionic Au16(2-) cluster has a stable, hollow, Td symmetric cage structure, stabilized by 18 delocalized valence electrons. The cage maintains its robust geometry, with a minor Jahn-Teller deformation, over several charge states (q = -1,0,+1), forming spin doublet, triplet and quadruplet states according to the Hund's rules. Endohedral doping of the Au16 cage by Al or Si yields a geometrically robust, tuneable oxidation and reduction agent. Si@Au16 is a magic species with 20 delocalized electrons. We calculate a significant binding energy for the anionic Si@Au16/O2- complex and show that the adsorbed O2 is activated to a superoxo-species, a result which is at variance with the experimentally well-documented inertness of Au16- anion towards oxygen uptake.

Journal Article↗
PubMed1968

Reduced nicotinamide adenine dinucleotide and the reduction of oxidized glutathione in human erythrocytes.

The ability of reduced nicotinamide adenine dinucleotide (NADH), generated through the activity of lactic acid dehydrogenase, to support the reduction of endogenous oxidized glutathione in intact human erythrocytes and in hemolysates was investigated. Rapid initial oxidation of endogenous reduced glutathione was effected with methyl phenylazoformate. Freshly obtained normal erythrocytes and erythrocytes deficient in glucose-6-phosphate dehydrogenase activity were unable to regenerate reduced glutathione upon incubation with lactate. Only normal erythrocytes were capable of reducing oxidized glutathione after preincubation with glucose, inosine, or a medium which promoted the synthesis of increased amounts of intracellular NAD. This regeneration of reduced glutathione could be explained by the generation of reduced nicotinamide adenine dinucleotide phosphate through the metabolism of accumulated phosphorylated intermediates of glycolysis. Hemolysates prepared from both normal erythrocytes and from erythrocytes deficient in glucose-6-phosphate dehydrogenase activity were able to reduce oxidized glutathione in the presence of added lactate and NAD. The results obtained indicated either an inability of the intact erythrocyte to utilize the NAD at the concentrations attained or an altered behavior of the system for the regeneration of reduced glutathione after lysis of the cell.

Journal Article↗
PubMed2003

Effects of oxidation and reduction on contractile function in skeletal muscle fibres of the rat.

This study investigated the effects of the oxidants hydrogen peroxide (H(2)O(2)) and 2,2'-dithiodipyridine (DTDP), and reductants, glutathione (GSH) and dithiothreitol (DTT), on the properties of the contractile apparatus of rat fast- and slow-twitch skeletal muscle fibres, in order to assess how oxidation affects muscle function. Skinned muscle fibres were activated in heavily-buffered Ca(2+) solutions. The force-[Ca(2+)] relationship before and after various treatments was fitted by a Hill curve described by the maximum Ca(2+)-activated force, pCa(50) (-log(10)[Ca(2+)] giving half-maximum force) and n(H) (the Hill coefficient). Exposing freshly skinned fibres to strong reducing conditions (i.e. 10 mM DTT or 5 mM GSH) had little if any effect on Ca(2+) sensitivity (pCa(50) or n(H)). The effect of oxidants H(2)O(2) and DTDP depended on whether the fibre was relaxed (in pCa > 9) or activated during the exposure. In both fast- and slow-twitch fibres a 5 min exposure to 10 mM H(2)O(2) at pCa > 9 had no effect on pCa(50), causing only a reduction in n(H). In contrast, when fast-twitch fibres were activated in the presence of 10 mM H(2)O(2) (or 100 microM DTDP) there was a substantial increase in pCa(50) (by approximately 0.06 and 0.1, respectively), as well as larger decreases in n(H) than occurred in relaxed fibres, with all effects being reversed by DTT (10 mM, 10 min). In slow-twitch soleus fibres, the activation-dependent effect of DTDP was even greater (pCa(50) increased by ~0.35), and it was found that the rate of reversal in DTT was also increased by activation. A separate important phenomenon was that fast-twitch fibres that had been oxidised with H(2)O(2) or DTDP (while either relaxed or activated) showed a paradoxical increase in Ca(2+) sensitivity (~0.04 and 0.25 increase in pCa(50), respectively) when briefly exposed to the endogenous reductant GSH (5 mM, 2 min). This effect was reversed by DTT or longer (> 20 min) exposure to GSH, did not occur in slow-twitch soleus fibres, and may contribute to post-tetanic potentiation in fast-twitch muscle. Maximum force was not affected by any of the above treatments, whereas exposure to a high concentration of DTDP (1 mM) did greatly reduce force production. These findings reveal a number of novel and probably important effects of oxidation on the contractile apparatus in skeletal muscle fibres.

2,2'-Dipyridyl↗
PubMed1975

Polarographic studies on ubiquinone-10 and rhodoquinone bound with chromatophores from Rhodospirillum rubrum.

Redox components bound with chromatophores of Rhodospirillum rubrum, and pure samples of ubiquinone-10 and rhodoquinone were studied polarographically at 24 degrees. In a mixture of ethanol and water (4 : 1, v/v) at pH 7, ubiquinone-10 and rhodoquinone had half-wave potentials (E1/2) OF +43 MV and -63 mV, respectively. For both quinones, values of the electron transfer number (n) were 2 , and plots of E1/2 versus pH formed straight lines with slopes of -30 mV/pH in the neutral pH range; thus, values of the proton transfer number (n-a) were estimated to be 1 for both quinones. When bound with chromatophores, ubiquinone-10 and rhodoquinone had E1/2 values of +50 mV (n=2) and -30 mV (n=2), respectively, at pH 7. Values of (n-a) were estimated to be 1 for ubiquinone-10 and 2 for rhodoquinone. A component (POC-170) thought to be one of the active center bacteriochlorophylls (Liac-890) was characterized; it has E1/2 value of -170 mV at pH 7 and its oxidation-reduction is possibly brought about by dehydrogenation-hydrogenation. Conceivably, the oxidation-reduction sites of ubiquinone-10, rhodoquinone and POC-170 partly, if not all, exist on the surface of chromatophore membrane or project outside the membrane, because of their accessibility to the polarographic electrode.

Bacterial Chromatophores↗
PubMedDate not supplied

A nitric oxide sensor using reduction current.

Nitric oxide (NO) has a wide range of biologic activity. Methods commonly used for the detection of biologically derived NO are indirect and measure only the amount of NO released during an interval of time. An electrochemical method available is capable of being direct and continuous but is subject to interference. The recent explosion of scientific research into NO activity requires better methods of NO detection. This article reports a new NO electrochemical sensing method and sensor design. The tip of the sensor is covered with a hydrophobic membrane and contains an internal electrolyte. Platinum is used for the working and counter electrodes and silver/silver bromide (Ag/AgBr) for the reference electrode. The components of the internal electrolyte are potassium bromide and sulfuric acid. The NO that diffuses to the working electrode is first oxidized to NO+; the NO+ is reduced to NO; and the reduction current is determined. An integrated pulsed amperometric method is used to achieve the redox of NO and the measurement and integration of the reduction current. The results show that the NO sensor is sensitive and has a rapid response and less interference.

Biosensing Techniques↗
PubMed1992

Effects of nitrate and nitrite on dissimilatory iron reduction by Shewanella putrefaciens 200.

The inhibitory effects of nitrate (NO3-) and nitrite (NO2-) on dissimilatory iron (FE3+) reduction were examined in a series of electron acceptor competition experiments using Shewanella putrefaciens 200 as a model iron-reducing microorganism. S. putrefaciens 200 was found to express low-rate nitrate reductase, nitrite reductase, and ferrireductase activity after growth under highly aerobic conditions and greatly elevated rates of each reductase activity after growth under microaerobic conditions. The effects of NO3- and NO2- on the Fe3+ reduction activity of both aerobically and microaerobically grown cells appeared to follow a consistent pattern; in the presence of Fe3+ and either NO3- or NO2-, dissimilatory Fe3+ and nitrogen oxide reduction occurred simultaneously. Nitrogen oxide reduction was not affected by the presence of Fe3+, suggesting that S. putrefaciens 200 expressed a set of at least three physiologically distinct terminal reductases that served as electron donors to NO3-, NO2-, and Fe3+. However, Fe3+ reduction was partially inhibited by the presence of either NO3- or NO2-. An in situ ferrozine assay was used to distinguish the biological and chemical components of the observed inhibitory effects. Rate data indicated that neither NO3- nor NO2- acted as a chemical oxidant of bacterially produced Fe2+. In addition, the decrease in Fe3+ reduction activity observed in the presence of both NO3- and NO2- was identical to the decrease observed in the presence of NO2- alone. These results suggest that bacterially produced NO2- is responsible for inhibiting electron transport to Fe3+.

Aerobiosis↗
PubMed1973

Oxidation and reduction of D-xylose by cell-free extract of Pichia quercuum.

The fermentation mechanism of the simultaneous production of D-xylonic acid and xylitol from D-xylose by Pichia quercuum was studied by using a cell-free enzyme preparation. Nicotinamide adenine dinucleotide phosphate (NADP)-dependent D-xylose dehydrogenase activity and NADP-dependent D-xylose reductase activity were detected, and the oxido-reduction reaction of D-xylose was able to couple through regeneration of NADP and NADPH to produce D-xylonic acid and xylitol.

Alcohol Oxidoreductases↗
PubMed2003

Diallyl sulfide inhibits the oxidation and reduction reactions of stilbene estrogens catalyzed by microsomes, mitochondria and nuclei isolated from breast tissue of female ACI rats.

Previously, it has been demonstrated that microsomal, mitochondrial and nuclear enzymes isolated from the liver of male Sprague-Dawley rats catalyzed the oxidation of diethylstilbestrol (DES) to DES quinone. In the present study we have shown that diallyl sulfide (DAS) inhibits the oxidation of DES to DES quinone in all three subcellular fractions (microsomes, mitochondria and nuclei) isolated from breast tissue of female ACI rats. UV analysis of mitochondrial and microsomal fractions revealed that DAS decreased the rate of DES oxidation to DES quinone and DAS also decreased the rate in which DES quinone was reduced to DES. Lineweaver-Burk plots of the rate of DES quinone formation at various DES and DAS concentrations demonstrated that DAS inhibited the oxidation of DES and the reduction of DES quinone in a non-competitive fashion. In both microsomal and mitochondrial oxidation reactions the K(m) remained constant whereas the V(max) decreased with increasing DAS (0, 186 and 373 microM) concentrations (microsomes K(m) = 80 microM; V(max) = 5.56, 4.16 and 3.33 nmol/mg protein/min; mitochondria K(m) = 35.7 microM; V(max) = 3.45, 2.44 and 1.82 nmol/mg protein/min). Results were similar for reduction reactions. HPLC analysis revealed that a concentration of 186 microM DAS inhibited the mitochondrial, microsomal and nuclear oxidation by 27, 35 and 40%, respectively. A concentration of 373 microM DAS inhibited the mitochondrial, microsomal and nuclear oxidation by 50, 52 and 60% respectively. The data provide direct evidence that the breast tissue contain the metabolic machinery required to oxidize DES to reactive intermediates that may lead to genetic instability and cancer. This inhibition may play a role in the chemoprevention of stilbene estrogen-induced breast cancer.

Allyl Compounds↗
PubMed1990

Oxidation and reduction of bile acid precursors by rat hepatic 3 alpha-hydroxysteroid dehydrogenase and inhibition by bile acids and indomethacin.

Enzyme kinetics of purified rat hepatic 3 alpha-hydroxysteroid dehydrogenase for bile acid precursors and effects of bile acids and indomethacin on those activities were studied. This enzyme catalyzed the oxidoreduction of the C3 position of bile acid precursors. Km for 7 alpha, 12 alpha-dihydroxy-5 beta-cholestan-3-one (1.6 microM) was markedly lower than Km for 7 alpha-hydroxy-5 beta-cholestan-3-one (28 microM) but Vmax was similar. Km for 3 alpha, 7 alpha-dihydroxy-5 beta-cholestane (12 microM) was lower than Km for 3 alpha, 7 alpha, 12 alpha-trihydroxy-5 beta-cholestane (150 microM) although Vmax/Km values were similar for both compounds. Bile acids and indomethacin inhibited the reduction of 3-oxo bile acid precursors. NADPH inhibited the binding of lithocholic acid (3 alpha-hydroxy-5 beta-cholanic acid) by 3 alpha-hydroxysteroid dehydrogenase. These data suggest that intrahepatic bile acid concentrations may affect the reduction of 3-oxo-bile acid precursors and intrahepatic redox conditions may affect intracellular bile acid transfer.

3-Hydroxysteroid Dehydrogenases↗
PubMed2002

Metalla-supramolecular rectangles as electron reservoirs for multielectron reduction and oxidation.

The electron-transfer capacity of molecular rectangle ions [Pt(II)(4)(PEt(3))(8)(mu-anth(2-))(2)(mu-L)(2)](4+) with anth = anthracene-1,8-diyl and L = 4,4'-bipyridine (bp) or 1,2-bis(4-pyridyl)ethene (bpe) was investigated in acetonitrile and dichloromethane using cyclic voltammetry, EPR, and UV-vis-near-IR spectroelectrochemistry. The compounds can be reversibly reduced, first in a two-electron process and then via two closely separated one-electron steps. Oxidation was also possible at rather low potentials in a reversible two-electron step, followed by an electrochemically irreversible process. The spectroscopic results indicate reduction at the neutral acceptor ligands L and oxidation at the formally dianionic anthracene "clips". In contrast, the prototypical molecular square ([Pt(triphos)(mu-bp)](4))(8+) undergoes only irreversible reduction.

Anthracenes↗
PubMed1998

Histochemical detection of quinone reductase activity in situ using LY 83583 reduction and oxidation.

The application of enzymatic staining techniques, using tetrazolium dyes, to aldehyde-treated brain sections has revealed the presence of NADPH-diaphorase activity attributed to nitric oxide synthase. When evaluating the specificity of the putative guanylyl cyclase inhibitor LY 83583, a robust and novel staining pattern was noted in epithelial, endothelial, and astrocytic cells when LY 83583 was included in the NADPH-diaphorase histochemical reaction. This LY 83583-dependent staining could be blocked by the NAD(P)H:quinone oxidoreductase inhibitor dicumarol. Based on its quinone structure, we hypothesized that LY 83583 was a substrate for the enzyme NAD(P)H:quinone oxidoreductase. Transfection of human embryonic kidney 293 cells with the rat liver isoform of NAD(P)H:quinone oxidoreductase resulted in robust NADPH- and LY 83583-dependent staining that was completely blocked by dicumarol and was not observed in untransfected cells. Analysis of transfected cell extracts and brain homogenates indicated that LY 83583 was a substrate for NAD(P) H:quinone oxidoreductase, with a Km similar to the well-characterized substrate menadione. Sensitivity of the nitroblue tetrazolium reduction to superoxide dismutase indicated that the reduction of LY 83583 by NAD(P)H:quinone oxidoreductase leads to superoxide generation. The localization of NAD(P)H:quinone oxidoreductase activity to astrocytic cells suggests a role for glia in combating oxidative insults to brain and in activating quinone-like drugs such as LY 83583.

Aminoquinolines↗