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1.
Jiajia Wu Huaiqun Liu Peng Wang Dun Zhang Yan Sun Ee Li 《Indian journal of microbiology》2017,57(3):344-350
Sulfate-reducing bacteria (SRB) were found to be capable of tolerating a certain amount of oxygen (O2), but how they affect oxygen reduction reaction (ORR) has not been clear. The present work investigated the impact of SRB on ORR in 3.5 wt% sodium chloride solution with the cyclic voltammetry method. The addition of SRB culture solution hampered both the reduction of O2 to superoxide (O 2 ·? ) and hydrogen peroxide (H2O2) to water (H2O), and the influence of SRB metabolites was much larger than that of bacterial cells. Sulfide and extracellular polymeric substances (EPS), typical inorganic and organic metabolic products, had great impact on ORR. Sulfide played an important role in the decrease of cathodic current for H2O2 reduction due to its hydrolysis and chemical reaction activity with H2O2. EPS were sticky, easy to adsorb on the electrode surface and abundant in functional groups, which hindered the transformation of O2 into O 2 ·? and favored the reduction of H2O2 to H2O. 相似文献
2.
A. S. Gorbunova M. M. Borisova-Mubarakshina I. A. Naydov S. S. Osochuk B. N. Ivanov 《Doklady. Biochemistry and biophysics》2018,483(1):355-358
The characteristics of the formation of the superoxide radical anion (\(\rm{O}_2^{\bullet-}\)) and hydrogen peroxide by xanthine oxidases isolated from microorganisms and from cow’s milk were investigated. The increase in pH led to an increase in the rate of xanthine oxidation with oxygen by both xanthine oxidases. The functioning of xanthine oxidase from milk along with the two-electron reduction of O2 to H2O2 carries through the one-electron reduction of O2 to \(\rm{O}_2^{\bullet-}\), and the rate and the fraction of generation of \(\rm{O}_2^{\bullet-}\) increased with increasing pH. Under operation of the microbial xanthine oxidase, the \(\rm{O}_2^{\bullet-}\) radical was not detected in the medium. The results suggest a difference in the operation of active centers of enzyme from different sources. 相似文献
3.
Oxidation of NADH by decavanadate, a polymeric form vanadate with a cage-like structure, in presence of rat liver microsomes followed a biphasic pattern. An initial slow phase involved a small rate of oxygen uptake and reduction of 3 of the 10 vanadium atoms. This was followed by a second rapid phase in which the rates of NADH oxidation and oxygen uptake increased several-fold with a stoichiometry of NADH: O2 of 11. The burst of NADH oxidation and oxygen uptake which occurs in phosphate, but not in Tris buffer, was prevented by SOD, catalase, histidine, EDTA, MnCl2 and CuSO4, but not by the hydroxyl radical quenchers, ethanol, methanol, formate and mannitol. The burst reaction is of a novel type that requires the polymeric structure of decavanadate for reduction of vanadium which, in presence of traces of H2O2, provides a reactive intermediate that promotes transfer of electrons from NADH to oxygen. 相似文献
4.
The inhibition patterns of rabbit sera (RS1 & RS2) from two different rabbits on the photosynthetic electron transport of isolated spinach thylakoids were studied. Fifty l of RSI were required for 100% inhibition of a H2O MV/O2 reaction, while only 10 l of a 1:10 dilution of RS2 were needed for 100% inhibition. The RS2 serum was greatly hemolyzed. The -globulin fraction from purified rabbit serum (RS1) did not inhibit photosynthetic electron transport, indicating that the antibody fraction of the rabbit serum does not contain the inhibitor. It appears that the inhibitor is from the hemolyzed red blood cells. Rabbit sera added prior to chloroplast illumination caused no inhibition, while addition of rabbit sera during illumination inhibited a H2O MV/O2 reaction within 1–3s. Aminotriazole, a catalase inhibitor, did not affect the efficacy of the rabbit sera indicating that the unknown rabbit serum inhibitor is not catalase. Various Hill reactions were employed to determine the site of inhibition. Rabbit sera inhibited the following reactions: DHQ/DCMU MV/O2, DAD/Asc/DBMIB MV/O2, and DCIP/Asc/DBMIB MV/O2. Rabbit sera did not inhibit a H2O DADox reaction indicating that inhibition is on the reducing side of PSI. However, a H2O Fd/NADP+ reaction was not inhibited by rabbit sera. NADP did not interfere with the ability of RS2 to inhibit a MV-mediated Mehler reaction. In simultaneously measured assays of Fd-mediated O2 and NADP+ reductions, RS2 serum inhibited the reduction of O2 by ferredoxin without inhibiting the reduction of NADP+. These results indicate the potential involvement of parallel (branched) electron transport of the reducing side of PSI in the reduction of oxygen.Abbreviations RS1 and RS2
Rabbit serum 1 and 2
- MV
methylviologen
- DCMU
3,4-dichlorophenyl-N,N-dimethylurea
- KFeCN
potassium ferricyanide
- DCIP
dichlorophenolindolphenol
- DAD
2,3,5,6-tetramethyl-p-phenylenediamine
- DHQ
tetramethyl-p-hydroquinone (durohydroquinone)
- MES
[2-(N-morpholino)-esthanesulfonic acid]
- HEPES
[N-2-hydroxyethyl piperazine-N-2-ethanesulfonic acid]
- DBMIB
dibromothymoquinone
- PSI and PSII
photosystem I and II
- Fd
ferredoxin
- Chl
chlorophyll
- Asc
ascorbate
- SOD
superoxide dismutase 相似文献
5.
Boris K. Semin Lira N. Davletshina Kirill N. Timofeev Il’ya I. Ivanov Andrei B. Rubin Michael Seibert 《Photosynthesis research》2013,117(1-3):385-399
Extraction of Ca2+ from the oxygen-evolving complex of photosystem II (PSII) in the absence of a chelator inhibits O2 evolution without significant inhibition of the light-dependent reduction of the exogenous electron acceptor, 2,6-dichlorophenolindophenol (DCPIP) on the reducing side of PSII. The phenomenon is known as “the decoupling effect” (Semin et al. Photosynth Res 98:235–249, 2008). Extraction of Cl? from Ca2+-depleted membranes (PSII[–Ca]) suppresses the reduction of DCPIP. In the current study we investigated the nature of the oxidized substrate and the nature of the product(s) of the substrate oxidation. After elimination of all other possible donors, water was identified as the substrate. Generation of reactive oxygen species HO, H2O2, and O 2 ·? , as possible products of water oxidation in PSII(–Ca) membranes was examined. During the investigation of O 2 ·? production in PSII(–Ca) samples, we found that (i) O 2 ·? is formed on the acceptor side of PSII due to the reduction of O2; (ii) depletion of Cl? does not inhibit water oxidation, but (iii) Cl? depletion does decrease the efficiency of the reduction of exogenous electron acceptors. In the absence of Cl? under aerobic conditions, electron transport is diverted from reducing exogenous acceptors to reducing O2, thereby increasing the rate of O 2 ·? generation. From these observations we conclude that the product of water oxidation is H2O2 and that Cl? anions are not involved in the oxidation of water to H2O2 in decoupled PSII(–Ca) membranes. These results also indicate that Cl? anions are not directly involved in water oxidation by the Mn cluster in the native PSII membranes, but possibly provide access for H2O molecules to the Mn4CaO5 cluster and/or facilitate the release of H+ ions into the lumenal space. 相似文献
6.
Summary The prominent spontaneous reaction of aminoethylcysteine ketimine in the neutral pH range is the concentration-dependent dimerization (Hermann, 1961). The carboxylated dimer first produced loses the free carboxyl yielding the more stable decarboxylated dimer (named simply the dimer in this note). In the search for a possible biochemical activity of this uncommon tricyclic compound we have assayed whether it could interact with oxygen reactive species (H2O2, O2
–,OH) thus exhibiting a scavenging effect of possible biomedical interest. The dimer interacts with H2O2 producing compounds detectable by chromatographic procedures. The presence of Fe2+ stimulates the oxidative reaction by yielding the hydroxyl radical (the Fenton reaction). Using the system xanthine oxidase-xanthine as superoxide producer, the dimer oxidation by O2
– has also been documented. Among the oxidation products the presence of taurine and cysteic acid has been established. Identification of remaining oxidation products and investigation of the possible function of the dimer as a biological scavenger of oxygen reactive species are now oncoming.Abbreviations HPLC
high performance liquid chromatography
- AAÅ
amino acid analyzer
- SOD
superoxide dismutase
- EDTA
ethylenediaminetetraacetic acid 相似文献
7.
Rolf A. Løvstad 《Biometals》2003,16(3):435-439
Xanthine oxidase reduces molecular oxygen to H2O2 and superoxide radicals during its catalytic action on xanthine, hypoxanthine or acetaldehyde. Ascorbate is catalytically oxidized by the superoxide radicals generated, when present in the reaction solution (Nishikimi 1975). The present study shows that iron ions markedly stimulate the enzyme dependent ascorbate oxidation, by acting as a red/ox-cycling intermediate between the oxidase and ascorbate. An apparent Km-value of 10.8 M characterized the iron stimulatory effect on the reaction at pH 6.0. Reduced transition-state metals can be oxidized by H2O2 through a Fenton-type reaction. Catalase was found to reduce the effect of iron on the enzyme dependent ascorbate oxidation, strongly suggesting that H2O2, produced during catalysis, is involved in the oxidation of ferrous ions. 相似文献
8.
P450cam (CYP101A1) is a bacterial monooxygenase that is known to catalyze the oxidation of camphor, the first committed step in camphor degradation, with simultaneous reduction of oxygen (O2). We report that P450cam catalysis is controlled by oxygen levels: at high O2 concentration, P450cam catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol. We confirmed, using 17O and 2H NMR, that the hydrogen atom added to camphor comes from water, which is oxidized to hydrogen peroxide (H2O2). This is the first time a cytochrome P450 has been observed to catalyze oxidation of water to H2O2, a difficult reaction to catalyze due to its high barrier. The reduction of camphor and simultaneous oxidation of water are likely catalyzed by the iron-oxo intermediate of P450cam, and we present a plausible mechanism that accounts for the 1∶1 borneol:H2O2 stoichiometry we observed. This reaction has an adaptive value to bacteria that express this camphor catabolism pathway, which requires O2, for two reasons: 1) the borneol and H2O2 mixture generated is toxic to other bacteria and 2) borneol down-regulates the expression of P450cam and its electron transfer partners. Since the reaction described here only occurs under low O2 conditions, the down-regulation only occurs when O2 is scarce. 相似文献
9.
Hubert G. D. Niekus Els van Doorn Adrian H. Stouthamer 《Archives of microbiology》1980,127(2):137-143
The kinetics of oxygen utilization by the microaerophile Campylobacter sputorum subspecies bubulus was studied. With formate as substrate two enzyme systems were found to be responsible for electron transfer between formate and oxygen. In the case of lactate oxidation one enzyme system could account for the activity measured. One of the formateoxidizing systems possessed a high affinity for oxygen [K
m(O2)=approx. 4M O2]. From inhibitor studies it was concluded that a respiratory chain was involved in its activity. Respiration by this system must be responsible for proton translocation and electron transport-linked phosphorylation at formate oxidation. The other enzyme system had an extremely low affinity for oxygen [K
m (O2)=approx. 1 mM O2]. It was tentatively identified as the H2O2-producing formate oxidase previously found in C. sputorum. The H2O2 production by this enzyme is implicated in an explanation of the microaerophilic nature of C. sputorum. Sensitivity of formate dehydrogenase to H2O2 was demonstrated. The influence of the formate concentration on aerobic formate oxidation was determined. The pH- and temperature dependencies of oxygen uptake with formate as substrate were examined at airsaturation and at a low dissolved oxygen tension.Abbreviations TL medium
tryptose-lactate medium
- TF medium
tryptose-formate medium
- HQNO
2-n-heptyl-4-hydroxyquinoline N-oxide
- SHAM
salicylhydroxamic acid
- DCPIP
2,6-dichlorophenolindophenol 相似文献
10.
Helmut Sies 《The Journal of biological chemistry》2014,289(13):8735-8741
Hydrogen peroxide, the nonradical 2-electron reduction product of oxygen, is a normal aerobic metabolite occurring at about 10 nm intracellular concentration. In liver, it is produced at 50 nmol/min/g of tissue, which is about 2% of total oxygen uptake at steady state. Metabolically generated H2O2 emerged from recent research as a central hub in redox signaling and oxidative stress. Upon generation by major sources, the NADPH oxidases or Complex III of the mitochondrial respiratory chain, H2O2 is under sophisticated fine control of peroxiredoxins and glutathione peroxidases with their backup systems as well as by catalase. Of note, H2O2 is a second messenger in insulin signaling and in several growth factor-induced signaling cascades. H2O2 transport across membranes is facilitated by aquaporins, denoted as peroxiporins. Specialized protein cysteines operate as redox switches using H2O2 as thiol oxidant, making this reactive oxygen species essential for poising the set point of the redox proteome. Major processes including proliferation, differentiation, tissue repair, inflammation, circadian rhythm, and aging use this low molecular weight oxygen metabolite as signaling compound. 相似文献
11.
underlying mechanism of ROS-induced cell injury remains to be defined. This study was undertaken to examine the role of lipid peroxidation and poly (ADP-ribose) polymerase (PARP) activation in H2O2-induced cell death in A172 cells, a human glioma cell line. H2O2 induced a dose- and time-dependent cell death. The cell death was prevented by thiols (dithiothreitol and glutathione), iron chelators (deferoxamine and phenanthroline), H2O2 scavengers (catalase and pyruvate), and a hydroxyl radical scavenger (dimethylthiourea). Antioxidants N,N-diphenyl-p-phenylenediamine (DPPD) and Trolox had no effect on the H2O2-induced cell death. Lipid peroxidation did not increase in human glioma cells exposed to H2O2. The PARP inhibitor 3-aminobenzamide prevented the cell death induced by H2O2. The PARP activity was increased by H2O2 and the H2O2 effect was prevented by 3-aminobenzamide, dithiothreitol, and phenanthroline. The ATP depletion induced by H2O2 was prevented by catalase, dithiothreitol, phenanthroline, and 3-aminobenzamide, but not by DPPD. These results indicate that the H2O2-induced cell death is mediated by PARP activation but not by lipid peroxidation in human glioma cells. 相似文献
12.
Polarographic Measurements of Spontaneous and Mitochondria-Promoted Oxidation of 5,6-and 5,7-Dihydroxytryptamine 总被引:1,自引:0,他引:1
Abstract: Spontaneous oxygen consumption by 5,6- and 5,7-DHT (dihydroxytryptamine), related indoleethylamines, and 6-hydroxydopamine and oxygen consumption by these compounds in the presence of rat liver mitochondria were measured by the polarographic oxygen electrode technique. 5,6- and 5,7-DHT react with oxygen at very different rates (2.7 nmol O2/min and 33.4 nmol O2/min, respectively) when incubated in buffer, pH 7.2, at a concentration of 1 mm and with different kínetic characteristics. While the oxidation of 5,7-DHT obeys a reaction of second-order type, the oxidation of 5,6-DHT is more complex and characterized by autocatalytic promotion. Coloured quinoidal oxidation products appeared during the degradation of both indoleamines. Glutathione, ascorbate, dithiothreitol, cysteine, albumin, and superoxide dismutase partially prevented 5,6- and 5,7-DHT from oxidative destruction. Catalase saved oxygen only in the case of 5,6-DHT by recycling of O2 released from near-stoichiometrically formed H2O2 during oxidation of 5,6-DHT: 5,7-DHT did not generate H2O2 in measurable amounts. Oxygen consumption rates of 5,6- and 5,7-DHT were enhanced after addition of rat liver mitochondria to the incubation medium; this resulted in an accelerated formation of quinoidal products. This stimulatory effect on the oxidation rates of both 5,6- and 5,7-DHT was blocked by cyanide, but not rotenone, and was abolished by boiling of the mitochondria fraction. The observed increase in oxygen consumption in the presence of mitochondria was found not to be influenced by monoamine oxidase-dependent deamination of 5,6- and 5,7-DHT. It is postulated that 5,6- and 5,7-DHT are capable of participating in the electron transfer of the mitochondrial respiration chain beyond complex III. Results obtained in determinations of ADP:0 ratios in respiratory control experiments exclude a possible interference of 5,6-DHT, 5,7-DHT, and 6-OH-DA with phosphorylating sites. During the activated state of respiration, no signs of electron transfer inhibition by 5,6- and 5,7-DHT were detectable. A comparison and evaluation of the autoxidation rates of various hydroxylated indoleethylamines, of their affinity to the 5-HT transport sites, and their neurotoxic potency in vivo reveals that interaction of these compounds with oxygen at restricted reaction velocity is a prerequisite for efficient toxicity in monoaminergic neurons following active accumulation in these neurons via the high-affinity uptake systems. 相似文献
13.
Summary The in vivo induction of H2O2 production was tested on tobacco cell suspension cultures (Nicotiana tabacum cv. Bright Yellow-2). The measurement of H2O2 was based on the oxidation of 3,5-dichloro-2-hydroxybenzensulfonic acid by endogenous peroxidases and spectrophotometric detection after reaction with 4-aminoanti-pyrine. The phosphatase inhibitor cantharidin induced a transient increase in H2O2 synthesis. The timing of the H2O2 production, the level of induction by cantharidin and the background H2O2 production were dependent on the tobacco cell concentration used. A concentration curve of cantharidin revealed saturating kinetics for the H2O2 detection (E50=46 to 70 M, Emax=101 to 128 mol/h·g fresh weight). An inhibitor study with the tobacco BY-2 cells showed high inhibitions of the H2O2 induction with the flavin analogues diphenylene iodonium (I50=1.26M) and acridine orange and with membrane-permeative thiol reagents (N-ethyl maleimide, N-pyrene maleimide, iodoacetate); whereas the nonpermeative thiol reagentp-chloromercuribenzoic acid was ineffective. Therefore, the induction of H2O2 production with phosphatase inhibitors (cantharidin) showed comparable properties to the elicitor-induced oxidative-burst response in other plant cells.Abbreviations AcOr
acridine orange
- AOS
active-oxygen species
- BY-2
Bright Yellow-2
- pCMBS
p-chloromercuribenzoic acid
- DHBS
3,5-dichloro-2-hydroxybenzenesulfonic acid
- DMSO
dimethylsulfoxide
- DPI
diphenylene iodonium
- EtOH
ethanol
- H2O2
hydrogen peroxide
- HRP
horseradish peroxidase
- MS
Murashige and Skoog
- NEM
N-ethyl maleimide
- NPM
N-pyrene maleimide
- O
2
–
superoxide
- SOD
superoxide dismutase 相似文献
14.
Junichi Mano Kunio Kawamoto G. Charles Dismukes Kozi Asada 《Photosynthesis research》1993,38(3):433-440
A new binding site for anions which inhibit the water oxidizing complex (WOC) of Photosystem II in spinach has been identified. Anions which bind to this site inhibit the flash-induced S2/S0 catalase reaction (2H2O22H2O+O2) of the WOC by displacing hydrogen peroxide. Using a mass spectrometer and gas permeable membrane to detect the 32O2 product, the yield and lifetime of the active state of the flash-induced catalase (to be referred to simply as flash-catalase) reaction were measured after forming the S2 or S0-states by a short flash. The increase in flash-catalase activity with H2O2 concentration exhibits a Km=10–20 mM, and originates from an increase in the lifetime by 20-fold of the active state. The increased lifetime in the presence of peroxide is ascribed to formation of the long-lived S0-state at the expense of the unstable S2-state. The anion inhibition site differs from the chloride site involved in stimulating the photolytic water oxidation reaction (2H2OO2+4e-+4H+). Whereas water oxidation requires Cl- and is inhibited with increasing effectiveness by F-CN-N3
-, the flash-catalase reaction is weakly inhibited by Cl-, and with increasing effectiveness by F-CN-, N3
-. Unlike water oxidation, chloride is unable to suppress or reverse inhibition of the flash-catalase reaction caused by these anions. The inhibitor effectiveness correlates with the pKa of the conjugate acid, suggesting that the protonated species may be the active inhibitor. The reduced activity arises from a shortening of the lifetime of the flash-induced catalase active state by 3–10 fold owing to stronger anion binding in the flash-induced states, S2 and S0, than in the dark S-states, S1 and S-1. To account for the paradoxical result that higher anion concentrations are required to inhibit at lower H2O2 concentrations, where S2 forms initially after the flash, than at higher H2O2 concentrations, where S0 forms initially after the flash, stronger anion binding to the S0-state than to the S2-state is proposed. A kinetic model is given which accounts for these equilibria with anions and H2O2. The rate constant for the formation/release of O2 by reduction of S2 in the WOC is <0.4 s-1.Abbreviations ADRY
acceleration of the deactivation reactions of the water splitting enzyme system Y
- BTP
bis [tris(hydroxymethyl)methylamino]-propane
- CCCP
carbonylcyanide m-chlorophenylhyrazone
- DCBQ
2,5-dichlorobenzoquinone
- DMBQ
2,3-dimethylbenzoquinone
- WOC
water oxidizing complex 相似文献
15.
The crude extracellular cellulase from Clostridium thermocellum was oxidatively inactivated by air and inhibited by sulfhydryl reagents. Activity-loss was prevented and reversed by the addition of a high concentration (10 mM) dithiothreitol (DDT) at zero time and up to 24 h respectively. In the presence of a low concentration (0.4 mM) of DTT, the enzyme was more rapidly inactivated than in air alone. This was probably due to autoxidation of the low DTT concentration to H2O2 as shown by its prevention by a high DTT concentration, exclusion of air, or catalase; and by the oxidative inactivation of the enzyme by H2O2. The inactivation by H2O2 could be prevented by a high concentration of DTT but not by air exclusion. EDTA protected the enzyme from inactivation in air by a low concentration of DTT or by H2O2. This is presumably due to the role of metals in oxidation of SH groups. Furthermore, copper (5 M) also caused inactivation and this was prevented by the presence of a high DTT concentration. Even in the protective atmosphere of a high DTT concentration, cellulase was inactivated by certain apolar chelating agents such as o-phenanthroline and -1-dipyridyl, such inactivation being preventable by the prior incubation of the chelator with a mixture of Fe2+ and Fe3+. These data suggest that the clostridial cellulase, unlike the enzyme from aerobic fungi, contains essential sulfhydryl groups and is stimulated by iron. The endo--glucanase component of the cellulase complex was not susceptible to oxidative inactivation.Abbreviations DTT
dithiothreitol
- CMC
carboxymethylcellulose
- DTNB
5,5-dithiobis-(2-nitrobenzoic acid)
- NEM
N-ethylmaleimide
-
p-CMB
p-chloromercuribenzoic acid 相似文献
16.
A derivative of Rhizobium japonicum (strain 122 DES) has been isolated which forms nodules on soybeans that evolve little or no H2 in air and efficiently fixes N2. Bacteroids isolated from nodules formed by strain 122 DES took up H2 with O2 as the physiological acceptor and appeared to be typical of those R. japonicum strains that possess the H2 uptake system. The hydrogenase system in soybean nodules is located within the bacteroids and activity in macerated bacteroids is concentrated in a particulate fraction. The pH optimum for the reaction is near 8.0 and apparent K
m values for H2 and O2 are 2 M and 1 M, respectively. The H2 oxidizing activity of a suspension of 122 DES bacteroids was stable at 4°C for at least 4 weeks and was not particularly sensitive to O2. Neither C2H2 nor CO inhibited O2 dependent H2 uptake activity.Non-physiological electron acceptors of positive oxidation reduction potential also supported H2 uptake by bacteroids. The rate of H2 uptake with phenazine methosulfate as the acceptor was greater than that with O2. When methylene blue, triphenyltetrazolium, potassium ferricyanide or dichlorophenolindophenol were added to bacteriod suspensions, without preincubation, rates of H2 uptake were supported that were lower than those in the presence of O2. Preincubation of the bacteroids with acceptors increased the rates of H2 uptake. No H2 evolution was observed from reaction mixtures containing bacteroid suspensions and reduced methyl or benzyl viologens. Of a series of carbon substrates added to bacteroid suspensions only acetate, formate or succinate at concentrations of 50 mM resulted in 20% or greater inhibition of H2 oxidation.The H2 uptake capacity of isolated 122 DES bacteroids (expressed on a dry bacteroid basis) was at least 10-fold higher than the rate of the nitrogenase reaction in nodules expressed on a comparable basis. Since about 1 mol of H2 is evolved for every mol of N2 reduced during the N2 fixation reaction, these observations explain why soybean nodules formed by strain 122 DES and other strains with high H2 uptake activities have a capacity for recycling all the H2 produced from the nitrogenase reaction.Abbreviations PMS
PHenazine methosulfate
- MB
Methylene blue 相似文献
17.
Cosso RG Turim J Nantes IL Almeida AM Di Mascio P Verces AE 《Journal of bioenergetics and biomembranes》2002,34(3):157-163
Pure singlet molecular oxygen (1O2) generated by thermal decomposition of the 3,3-(1,4-naphthylidene) dipropionate endoperoxide (NDPO2), inhibited respiration of isolated rat liver mitochondria supported by NADH-linked substrates or succinate, but not by N,N,N,N-tetramehyl-p-phenylene-diamine (TMPD)/ascorbate. Under the latter conditions, mitochondria treated with 2.7 mM NDPO2 exhibited a decrease in transmembrane potential () in manner dependent on NDPO2 exposure time. This process was sensitive to the mitochondrial permeability transition inhibitors EGTA, dithiothreitol, ADP, and cyclosporin A. The presence of deuterium oxide (D2O), that increases 1O2 lifetime, significantly enhanced NDPO2-promoted mitochondrial permeabilization. In addition, NDPO2-induced mitochondrial permeabilization was accompanied by DTT or ADP-sensitive membrane protein thiol oxidation. Taken together, these results provide evidence that mitochondrial permeability transition induced by chemically generated singlet oxygen is mediated by the oxidation of membrane protein thiols. 相似文献
18.
Argante Bozzi Irene Mavelli Alessandro Finazzi Agrò Roberto Strom Anna Maria Wolf Bruno Mondovi Giuseppe Rotilio 《Molecular and cellular biochemistry》1976,10(1):11-16
Summary The enzymatic destruction of oxidizing products produced during metabolic reduction of oxygen in the cell (such as singlet oxygen, H2O2 and OH radical) involves the concerted action of superoxide dismutase-which removes O
2
-
and yields H2O2-and H2O2 removing enzymes such as catalase and glutathione peroxidase. A difference in distribution or ratio of these enzymes in various tissues may result in a different reactivity of oxygen radicals.It was found that in red blood cells superoxide dismutase and catalase are extracted in the same fraction as hemoglobin, while glutathione peroxidase appears to be loosely bound to the cellular structure. This suggests that in red blood cells catalase acts in series with superoxide dismutase against bursts of oxygen radicals formed from oxyhemoglobin, while glutathione & peroxidase may protect the cell membrane against low concentrations of H2O2. On the other hand, catalase activity is absent in various types of ascites tumor cells, while glutathione peroxidase and superoxide dismutase are found in the cytoplasm. However, the peroxidase/dismutase ratio is lower than in liver cells, and this may provide an explanation for the higher susceptibility of tumor cells to treatments likely to involve oxygen radicals. 相似文献
19.
Ronald S. Pardini 《Archives of insect biochemistry and physiology》1995,29(2):101-118
The survival of all aerobic life forms requires the ground-state of molecular oxygen, O2. However, the activation of O2 to reactive oxygen species (ROS) is responsible for universal toxicity. ROS are responsible in deleterious intracellular reactions associated with oxidative stress including membrane lipid peroxidation, and the oxidation of proteins and DNA. Redox-active allelochemicals such as quinones and phenolic compounds are involved in activating O2 to its deleterious forms including superoxide anion free radical, $ {\rm O}_{\rm 2} ^{ \cdot - } $, hydrogen peroxide, H2O2, and hydroxyl radical, $ \cdot {\rm OH} $. Molecular oxygen is also activated in biologically relevant photosensitizing reactions to the singlet form, 1O2. The insect lifestyle exposes them to a broad diversity of pro-oxidant allelochemicals and, like mammalian species, they have developed an elaborate antioxidant system comprised of chemical antioxidants and a bank of antioxidant enzymes. We have found that an insect's antioxidant adaptation to a particular food correlates well with its risk of exposure to potential pro-oxidants. © 1995 Wiley-Liss, Inc. 相似文献
20.
M. W. Ahmed S. Choi K. Lyakhov U. Shaislamov R. K. Mongre D. K. Jeong R. Suresh H. J. Lee 《Plasma Physics Reports》2017,43(3):381-392
Plasma discharge is a novel disinfection and effectual inactivation approach to treat microorganisms in aqueous systems. Inactivation of Gram-negative Escherichia coli (E. coli) by generating high-frequency, high-voltage, oxygen (O2) injected and hydrogen peroxide (H2O2) added discharge in water was achieved. The effect of H2O2 dose and oxygen injection rate on electrical characteristics of discharge and E. coli disinfection has been reported. Microbial log reduction dependent on H2O2 addition with O2 injection was observed. The time variation of the inactivation efficiency quantified by the log reduction of the initial E. coli population on the basis of optical density measurement was reported. The analysis of emission spectrum recorded after discharge occurrence illustrated the formation of oxidant species (OH?, H, and O). Interestingly, the results demonstrated that O2 injected and H2O2 added, underwater plasma discharge had fabulous impact on the E. coli sterilization. The oxygen injection notably reduced the voltage needed for generating breakdown in flowing water and escalated the power of discharge pulses. No impact of hydrogen peroxide addition on breakdown voltage was observed. A significant role of oxidant species in bacterial inactivation also has been identified. Furthermore the E. coli survivability in plasma treated water with oxygen injection and hydrogen peroxide addition drastically reduced to zero. The time course study also showed that the retardant effect on E. coli colony multiplication in plasma treated water was favorable, observed after long time. High-frequency underwater plasma discharge based biological applications is technically relevant and would act as baseline data for the development of novel antibacterial processing strategies. 相似文献