Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: DrugBank:EXPT00568 (ascorbate)
 23,072 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fraction 2 (grana-stack) particles prepared with the French press showed absorbance changes, at room temperature and with sodium ascorbate and methyl-viologen, that were produced by the oxidation of cytochrome b-559. This oxidation was inhibited by 3-(3,4-dichlorophenyl)-1,1-dimethylurea (DCMU) and sensitized by system II of photosynthesis. The oxidation is too slow to account for the rates of the Hill reaction that have been observed with nicotinamide-adenine dinucleotide phosphate (NADP(+)). It appears that this cytochrome is not functioning in the main pathway of electron transport. In the presence of 2,3,5,6-tetramethyl-p-phenylene-diamine (DAD) and ascorbate, light-induced oxidation of cytochrome f took place within 3 msec (or faster) in the grana-stack particles. Treatment with the detergent Triton X-100 disrupted this rapid cytochrome f oxidation as well as the oxidation of cytochrome b-559. Subsequent plastocyanin addition did not restore the rapid oxidation of cytochrome f (nor of cytochrome b-559) but only slow changes of cytochrome f. In view of the fact that these particles contain almost no plastocyanin, it is unlikely that plastocyanin functions in electron transport between cytochrome f and P-700 in the particles derived from the grana-stack regions of the chloroplast.
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PMID:Electron transport reactions in grana preparations from spinach chloroplasts. 503 43

Spinach chloroplasts were found to contain three forms of cytochrome b(559) that have the same alpha-peak at 559 nm, but are distinguished from one another by their oxidation-reduction potentials. The high-potential (H) form (E(m) about 330-350 mV) is reducible by hydroquinone, the middle-potential (M) form (E(m) about 50-80 mV) is reducible by ascorbate but not by hydroquinone, and the low-potential (L) form is reducible by dithionite but not by ascorbate. The H form was the predominant one in freshly prepared chloroplasts and was strongly correlated with Photosystem II activity. Chloroplast treatments such as aging, sonication, and mild heating, singly or in combination, brought about a shift of the H to the M form. More drastic treatments resulted in shifts of the H and M forms to the L form. The role of cytochrome b(559) as an electron carrier in System II of plant photosynthesis is discussed.
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PMID:Three forms of cytochrome b 559 and their relation to the photosynthetic activity of chloroplasts. 528 50

Three functionally different cytochrome b redox centres, apparently of high metabolic activity, were detected in intact pigeon heart mitochondria; cytochrome b(1), b(m) and b(h), with maxima of absorption at 556.6 (State 5), 560.6, and 564.5 nm, respectively (alpha-bands, 77K). 2. Cytochrome (b(l) was reduced in the presence of either antimycin or HQNO (2-heptyl-4-hydroxyquinoline N-oxide). The absorption maximum was shifted by dithionite, cyanide, NNN'N'-tetramethyl-p-phenylenediamine + ascorbate, HQNO and antimycin. The spectra obtained on simultaneous or successive addition of HQNO and antimycin favoured the assumption of a common binding site for the two inhibitors. 3. Cytochrome b(m) was reduced in the presence of HQNO, but not in the presence of antimycin. No shifts of absorption maximum was observed. 4. Cytochrome b(h) was reduced in the presence of antimycin. HQNO was unable to cause reduction of this cytochrome by endogenous substrates. The absorption maximum was shifted to lower wavelength by organic solvents. It was inseparable from that of cytochrome b(m) in the presence of 0.4% ethanol. 5. The pattern of reduction in the presence of HQNO or antimycin demonstrates the functional difference of the three redox centres and appears incompatible wih a linear respiratory chain.
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PMID:Three functionally different cytochrome b redox centres in pigeon heart mitochondria. 612 15

Coupled phosphorylation was examined in liver, kidney and brain mitochondria from rats made thyrotoxic by injecting repeated doses of triiodothyronine. Liver and kidney mitochondria were maximally affected under these conditions, whereas effects on brain mitochondria were marginal. State-3 respiration rates with succinate decreased considerably in all the tissues, whereas glutamate oxidation increased in liver, but decreased in kidney and brain mitochondria. Oxidation rates of beta-hydroxybutyrate decreased in kidney and brain mitochondria but were not significantly affected in liver mitochondria. Oxidation of ascorbate + TMPD was not affected. State-4 respiration rates increased in general with all the substrates resulting in lowering of the RCI. The ADP/O ratios decreased in a site-specific manner in the mitochondria from the three tissues. The content of cytochrome b decreased in all three tissues, whereas the content of cytochrome c + c1 increased in liver and kidney but decreased in brain. The content of cytochrome a, however, was not significantly affected. Basal and Mg2+-stimulated ATPase activities increased in mitochondria of liver and kidney but not in those of brain; total ATPase activities, however, were not altered. The results imply that excessive levels of thyroid hormones over normal in the serum can lead to impairment of mitochondrial energy metabolism in a tissue-specific manner.
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PMID:Effect of experimental thyrotoxicosis on oxidative phosphorylation in rat liver, kidney and brain mitochondria. 621 75

Studies of hepatic submitochondrial particles, which provide an experimental system allowing direct measurements of electron transfer independent of substrate transport reactions, showed that chronic ethanol ingestion (36% calories, 40 days) lowered the specific respiratory rates associated with substrate oxidation. NADH oxidase activity was decreased about 40%, succinoxidase was decreased 25%, and oxidation in ascorbate mediated by phenazine methosulfate was decreased 20%. The content of dithionite-reducible cytochrome aa3 was decreased 38%, while that of cytochrome b was decreased 8%, and that of cytochromes c + c1 was decreased 14%. Steady state kinetic measurements indicated that the turnover number of cytochrome oxidase was unchanged, about 15 s-1 under uncoupled conditions with NADH as substrate. When electron flux to cytochrome c was maximal, cytochrome c was maintained in a more highly reduced state relative to cytochrome aa3 in submitochondrial particles from the ethanol-treated rat compared to those from the control rat. This finding is consistent with the greater decrease in cytochrome aa3 content relative to that of cytochrome c. The results indicate that the diminished content of cytochrome oxidase is one of the factors responsible for the lower respiration rates caused by chronic ethanol consumption.
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PMID:Effects of chronic ethanol consumption on the respiratory chain of rat liver submitochondrial particles. 625 68

Cell suspensions of Campylobacter fetus subsp. intestinalis grown microaerophilically in complex media consumed oxygen in the presence of formate, succinate, and DL-lactate, and membranes had the corresponding dehydrogenase activities. The cells and membranes also had ascorbate-N,N,N',N'-tetramethyl-p-phenylenediamine oxidase activity which was cyanide sensitive. The fumarate reductase activity in the membranes was inhibited by p-chloromercuriphenylsulfonate, and this enzyme was probably responsible for the succinate dehydrogenase activity. Cytochrome c was predominant in the membranes, and a major proportion of this pigment exhibited a carbon monoxide-binding spectrum. Approximately 60% of the total membrane cytochrome c, measured with dithionite as the reductant, was also reduced by ascorbate-N,N,N',N'-tetramethyl-p-phenylenediamine. A similar proportion of the membrane cytochrome c was reduced by succinate under anaerobic conditions, whereas formate reduced more than 90% of the total cytochrome under these conditions. 2-Heptyl-4-hydroxyquinoline-N-oxide inhibited reduction of cytochrome c with succinate, and the reduced spectrum of cytochrome b became evident. The inhibitor delayed reduction of cytochrome c with formate, but the final level of reduction was unaffected. We conclude that the respiratory chain includes low- and high-potential forms of cytochromes c and b; the carbon monoxide-binding form of cytochrome c might function as a terminal oxidase.
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PMID:Respiratory systems and cytochromes in Campylobacter fetus subsp. intestinalis. 625 51

Maximum growth of Campylobacter fetus subsp. jejuni, strain C-61, occurred when the cultures were incubated with shaking in atmospheres containing approximately 30% hydrogen, 5% oxygen, and 10% CO2. Suspensions of cells grown under these conditions consumed oxygen with formate as the substrate in the presence of 0.33 mM cyanide, which completely inhibited respiration with ascorbate-N,N,N',N'-tetramethyl-p-phenylenediamine and with lactate. Spectroscopic evidence with intact cells suggested that a form of cytochrome c, reducible with formate but not with lactate or ascorbate-N,N,N',N'-tetramethyl-p-phenylenediamine, can be reoxidized by a cyanide-insensitive system. Analysis of membranes from the cells showed high- and low-potential forms of cytochrome c, cytochrome b, and various enzymes, including hydrogenase, formate dehydrogenase, and fumarate reductase. The predominant carbon monoxide-binding pigment appeared to be a form of cytochrome c, but the spectra also showed evidence of cytochrome o. The membrane cytochromes were reduced by hydrogen in the presence of 2-heptyl-4-hydroxyquinoline-N-oxide at concentrations which prevented the reduction of cytochrome c with succinate as the electron donor. Reoxidation of the substrate-reduced cytochromes by oxygen was apparently mediated by cyanide-sensitive and cyanide-insensitive systems. The membranes also had hydrogen-fumarate oxidoreductase activity mediated by cytochrome b. We conclude that C. fetus jejuni has high- and low-potential forms of cytochrome which are associated with a complex terminal oxidase system.
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PMID:Aerobic and anaerobic respiratory systems in Campylobacter fetus subsp. jejuni grown in atmospheres containing hydrogen. 628 61

Membranes from free-living Rhizobium japonicum were isolated to study electron transport components involved in H2 oxidation. The H2/O2 uptake rate ratio in membranes was approximately 2. The electron transport inhibitors antimycin A, cyanide, azide, hydroxylamine, and 2-n-heptyl-4-hydroxyquinoline-N-oxide (HQNO) inhibited H2 uptake and H2-dependent O2 uptake significantly. H2-reduced minus O2-oxidized absorption difference spectra revealed peaks at 551.5, 560, and 603 nm, indicating the involvement of cytochromes c, b, and a-a3, respectively. H2-dependent cytochrome reduction was completely inhibited in the presence of 0.15 mM HQNO. This inhibition was relieved by the addition of 0.1 mM menadione. Evidence is presented for the involvement of two b-type cytochromes in H2 oxidation. One b-type cytochrome was not reduced by ascorbate and had an absorption peak at 560 nm. The reduction of this cytochrome by H2 was not inhibited by cyanide. A second b-type cytochrome, cytochrome b', was not reduced by H2 in the presence of cyanide. This cytochrome had an absorption peak at 558 nm. Carbon monoxide difference spectra with H2 as reductant provided evidence for the involvement of cytochrome o as well as cytochrome a3 in H2 oxidation. H2 uptake activity in cell-free extracts was inhibited by UV light irradiation. Most of the activity of the UV-treated extracts was restored with the addition of ubiquinone. The restored activity was inhibited by cyanide. A branched electron transport pathway from H2 to O2 is proposed.
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PMID:Electron transport components involved in hydrogen oxidation in free-living Rhizobium japonicum. 628 65

The pK and mid-point redox potential of the Q-analogue 7-(n-heptadecyl)mercapto-6-hydroxy-5,8-quinolinequinone (HMHQQ) in aqueous medium are so low that under the experimental conditions used for studying the inhibition of electron transfer in submitochondrial particles only the oxidized, anionic form is present. The KD of the analogue, determined by comparing its inhibitory effect with that of n-heptyl-4-hydroxyquinoline N-oxide, is (0.003 + 0.24 x mg protein/ml) microM. The inhibition of succinate oxidation is pH dependent, due to a pH-dependent change in the overcapacity of the QH2-oxidizing system above the Q-reducing system. If the terminal part of the respiratory chain is reduced with ascorbate, the analogue inhibits the reduction of cytochrome b by substrate in the presence of antimycin with a similar KD value. In the absence of ascorbate the KD value is 100-times higher. The reduction of cytochrome b by substrate in particles treated with 2,3-dimercaptopropanol (BAL) + O2 is also sensitive to HMHQQ, with a KD value in between the two values given above. It is concluded that the QH2 oxidase system contains two different sites for interaction with ubiquinone. The site responsible for the inhibition of steady-state electron transfer is near the Fe-S cluster, as is shown by the sensitivity to the redox state of this cluster and by the effect of HMHQQ on the EPR signal of the reduced cluster. The second site, which is similar to the antimycin-binding site, is occupied only at higher concentrations of inhibitor. The affinity of HMHQQ for this site is not affected by the redox state of the Fe-S cluster.
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PMID:Identification of two different Q-binding sites in QH2-cytochrome c oxidoreductase, using the Q analogue n-heptadecylmercapto-6-hydroxy-5,8-quinolinequinone. 629 2

The triphasic course previously reported for the reduction of cytochrome b in the succinate-cytochrome c reductase by either succinate or duroquinol has been shown to be dependent on the redox state of the enzyme preparation. Prior reduction with increasing concentrations of ascorbate leads to partial reduction of cytochrome c1, and a gradual decrease in the magnitude of the oxidation phase of cytochrome b. At an ascorbate concentration sufficient to reduce cytochrome c1 almost completely, the reduction of cytochrome b by either succinate or duroquinol becomes monophasic. Owing to the presence of a trace amount of cytochrome oxidase in the reductase preparation employed, the addition of cytochrome c makes electron flow from substrate to oxygen possible. Under such circumstances, the addition of a limited amount of either succinate or duroquinol leads to a multiphasic reduction and oxidation of cytochrome b. After the initial three phases as described previously, cytochrome b becomes oxidized before cytochrome c1 when the limited amount of added substrate is being used up. However, at the end of the reaction when cytochrome c1 is being rapidly oxidized, cytochrome b becomes again reduced. The above observations support a cyclic scheme of electron flow in which the reduction of cytochrome b proceeds by two different routes and its oxidation controlled by the redox state of a component of the respiratory chain.
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PMID:Multiphasic oxidation-reduction of cytochrome b in the succinate-cytochrome c reductase. 629 71


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