scholarly journals NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH–ubiquinone reductase preparation

1979 ◽  
Vol 180 (1) ◽  
pp. 129-135 ◽  
Author(s):  
Koichiro Takeshige ◽  
Shigeki Minakami
Keyword(s):  
Respiratory Chain ◽  
Complex I ◽  
Inorganic Salts ◽  
Superoxide Anions ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Sensitive Site ◽  
Effects Of Ph ◽  
High Concentrations ◽  
O2 Production

1. Both NADH and NADPH supported the oxidation of adrenaline to adrenochrome in bovine heart submitochondrial particles. The reaction was completely inhibited in the presence of superoxide dismutase, suggesting that superoxide anions (O2−) are responsible for the oxidation. The optimal pH of the reaction with NADPH was at pH7.5, whereas that with NADH was at pH9.0. The reaction was inhibited by treatment of the preparation with p-hydroxymercuribenzoate and stimulated by treatment with rotenone. Antimycin A and cyanide stimulated the reaction to the same extent as rotenone. The NADPH-dependent reaction was inhibited by inorganic salts at high concentrations, whereas the NADH-dependent reaction was stimulated. 2. Production of O2− by NADH–ubiquinone reductase preparation (Complex I) with NADH or NADPH as an electron donor was assayed by measuring the formation of adrenochrome or the reduction of acetylated cytochrome c which does not react with the respiratory-chain components. p-Hydroxymercuribenzoate inhibited the reaction and rotenone stimulated the reaction. The effects of pH and inorganic salts at high concentrations on the NADH- and NADPH-dependent reactions of Complex I were essentially similar to those on the reactions of submitochondrial particles. 3. These findings suggest that a region between a mercurialsensitive site and the rotenone-sensitive site of the respiratory-chain NADH dehydrogenase is largely responsible for the NADH- and NADPH-dependent O2− production by the mitochondrial inner membranes.

scholarly journals Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

1980 ◽  
Vol 191 (2) ◽  
pp. 421-427 ◽  
Author(s):  
J F Turrens ◽  
A Boveris
Keyword(s):  
Cytochrome B ◽  
Nadh Dehydrogenase ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Biphasic Effect ◽  
Carbonyl Cyanide ◽  
Autocatalytic Process ◽  
Ph Range ◽  
Energy Dependent ◽  
O2 Production

Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +/- 0.1 nmol of O2-/min per mg of protein at pH 7.4 and at 30 degrees C. When NADH is used as substrate, rotenone, antimycin and cyanide increase O2- production. In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site. The generation of O2- by the rotenone, the uncoupler carbonyl cyanide rho-trifluoromethoxyphenylhydrazone and oligomycin at concentrations similar to those required to inhibit energy-dependent succinate-NAD reductase. Cyanide did not affect O2- generation at the NADH dehydrogenase, but inhibited O2- production at the ubiquinone-cytochrome b site. Production of O2- at the NADH dehydrogenase is about 50% of the O2- generation but the ubiquinone-cytochrome b area at pH 7.4. Additivity of the two mitochondrial sites of O2- generation was observed over the pH range from 7.0 to 8.8. AN O2–dependent autocatalytic process that requires NADH, submitochondrial particles and adrenaline is described.

scholarly journals Dehydroepiandrosterone Inhibits Complex I of the Mitochondrial Respiratory Chain and is Neurotoxic In Vitro and In Vivo at High Concentrations

2006 ◽  
Vol 93 (2) ◽  
pp. 348-356 ◽  
Author(s):  
Dzhamilja Safiulina ◽  
Nadezhda Peet ◽  
Enn Seppet ◽  
Alexander Zharkovsky ◽  
Allen Kaasik
Keyword(s):  
Respiratory Chain ◽  
Complex I ◽  
Mitochondrial Respiratory Chain ◽  
High Concentrations ◽  
Mitochondrial Respiratory

scholarly journals NADH- and NADPH-dependent lipid peroxidation in bovine heart submitochondrial particles. Dependence on the rate of electron flow in the respiratory chain and an antioxidant role of ubiquinol

1980 ◽  
Vol 192 (3) ◽  
pp. 853-860 ◽  
Author(s):  
R Takayanagi ◽  
K Takeshige ◽  
S Minakami
Keyword(s):  
Lipid Peroxidation ◽  
Respiratory Chain ◽  
Electron Flow ◽  
Antimycin A ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Malondialdehyde Formation ◽  
Low Rate ◽  
Liquid Peroxidation

Malondialdehyde formations by bovine heart submitochondrial particles supported by NADH or NADPH in the presence of ADP and FeCl3 was studied. The NADH-dependent reaction was maximal at very low rate of electron input from NADH to the respiratory chain and it decreased when the rate became high. The reaction was stimulated by rotenone and inhibited by antimycin A when the input was fast, whereas it was not affected by the inhibitors when the input was slow. The input rate of the electrons from NADPH was also so low that the reaction supported by NADPH was not affected by the inhibitors. Most of the endogenous ubiquinone in the particles treated with antimycin A was reduced by NADH even in the presence of ADP-Fe3+ chelate, but uniquinone was not reduced by NADPH when ADP-Fe3+ was present. Succinate strongly inhibited both NADH- and NADPH-dependent lipid peroxidation. The inhibition was abolished when uniquinone was removed from the particles, and it appeared again when uniquinone was reincorporated into the particles. Reduced uniquinone-2 also inhibited the peroxidation, but duroquinol, which reduces cytochrome b without reducing endogenous uniquinone, did not. Thus the malondialdehyde formation appeared to be inversely related to the extent of the reduction of endogenous uniquinone. These observations suggest that both NADH- and NADPH-dependent liquid-peroxidation reactions are closely related to the respiratory chain and that the peroxidation is controlled by the concentration of reduced ubiquinone.

scholarly journals An analysis of the polypeptide composition of bovine heart mitochondrial NADH-ubiquinone oxidoreductase by two-dimensional polyacrylamide-gel electrophoresis

1979 ◽  
Vol 181 (2) ◽  
pp. 435-443 ◽  
Author(s):  
C Heron ◽  
S Smith ◽  
C I Ragan
Keyword(s):  
Gel Electrophoresis ◽  
Complex I ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Two Dimensional ◽  
Submitochondrial Particles ◽  
Ubiquinone Oxidoreductase ◽  
Bovine Heart ◽  
Nadh Ubiquinone Oxidoreductase

Purified preparations of Complex I (NADH-ubiquinone oxidoreductase) from bovine heart mitochondria may be resolved into 26 polypeptides by two-dimensional analysis combining isoelectric focusing and polyacrylamide-gel electrophoresis in sodium dodecyl sulphate. Similar analyses of the fragments obtained from chaotropic resolution of the enzyme show that each of these fragments contains a distinct and non-overlapping set of polypeptides. Evidence that the polypeptides seen in the intact enzyme are true constituents comes from analyses of immunoprecipitates obtained by allowing Complex I or solubilized submitochondrial particles to react with antisera directed against the whole enzyme and a subfragment of the enzyme.

scholarly journals Assembly of a chimeric respiratory chain from bovine heart submitochondrial particles and cytochromebdterminal oxidase ofEscherichia coli

FEBS Letters ◽  
2009 ◽  
Vol 583 (8) ◽  
pp. 1287-1291 ◽  
Author(s):  
Eleonora V. Gavrikova ◽  
Vera G. Grivennikova ◽  
Vitaliy B. Borisov ◽  
Gary Cecchini ◽  
Andrei D. Vinogradov
Keyword(s):  
Respiratory Chain ◽  
Ofescherichia Coli ◽  
Submitochondrial Particles ◽  
Bovine Heart

scholarly journals Lipid peroxidation and the reduction of ADP-Fe3+ chelate by NADH-ubiquinone reductase preparation from bovine heart mitochondria

1980 ◽  
Vol 192 (3) ◽  
pp. 861-866 ◽  
Author(s):  
K Takeshige ◽  
R Takayanagi ◽  
S Minakami
Keyword(s):  
Lipid Peroxidation ◽  
Complex I ◽  
Nadh Dehydrogenase ◽  
Reductase Activity ◽  
Thiol Group ◽  
Submitochondrial Particles ◽  
Essential Step ◽  
Sensitive Site ◽  
Mitochondrial Lipids ◽  
Optimal Ph

The NADH-ubiquinone reductase preparation (Complex I) of bovine hart mitochondria catalysed in the presence of reduced coenzymes and ADP-Fe3+ the lipid peroxidation of liposomes prepared from mitochondrial lipids. The apparent Km values for the coenzymes and the optimal pH of the reactions agreed well with those of the lipid peroxidation of the submitochondrial particles treated with rotenone. On assay of the reduction of ADP-Fe3+ chelate by the reduction of cytochrome c in the presence of superoxide dismutase and antimycin A or by the oxidation of reduced coenzymes, the reactions were not affected by rotenone but were inhibited by thiol-group inhibitors. The properties of the ADP-Fe3+ reductase activity were highly consistent with those of the lipid-peroxidation reaction. These observations suggest that electrons from reduced coenzymes are transferred to ADP-Fe3+ chelate from a component between a mercurial-sensitive site and the rotenone-sensitive one of the NADH dehydrogenase and that the reduction of ADP-Fe3+ chelate by the NADH dehydrogenase is an essential step in the lipid peroxidation.

Steady-State Kinetics of the Reduction of Coenzyme Q Analogs by Complex I (NADH:Ubiquinone Oxidoreductase) in Bovine Heart Mitochondria and Submitochondrial Particles†

Biochemistry ◽  
1996 ◽  
Vol 35 (8) ◽  
pp. 2705-2716 ◽  
Author(s):  
Romana Fato ◽  
Ernesto Estornell ◽  
Salvatore Di Bernardo ◽  
Francesco Pallotti ◽  
Giovanna Parenti Castelli ◽  
...  
Keyword(s):  
Steady State ◽  
Complex I ◽  
Coenzyme Q ◽  
Heart Mitochondria ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Steady State Kinetics ◽  
Kinetics Of

Efficient Preconcentration of Cu2+, Zn2+ and Fe3+ with an Agarose-Schiff Base Sorbent

2007 ◽  
Vol 72 (7) ◽  
pp. 908-916 ◽  
Author(s):  
Payman Hashemi ◽  
Hatam Hassanvand ◽  
Hossain Naeimi
Keyword(s):  
Schiff Base ◽  
Metal Ions ◽  
Metal Ion ◽  
Good Accuracy ◽  
Kinetic Studies ◽  
Sample Volume ◽  
Effects Of Ph ◽  
Glass Column ◽  
High Concentrations ◽  
Ph Range

Sorption and preconcentration of Cu2+, Zn2+ and Fe3+ on a salen-type Schiff base, 2,2'- [ethane-1,2-diylbis(nitrilomethylidyne)]bis(2-methylphenol), chemically immobilized on a highly crosslinked agarose support, were studied. Kinetic studies showed higher sorption rates of Cu2+ and Fe3+ in comparison with Zn2+. Half-times (t1/2) of 31, 106 and 58 s were obtained for sorption of Cu2+, Zn2+ and Fe3+ by the sorbent, respectively. Effects of pH, eluent concentration and volume, ionic strength, buffer concentration, sample volume and interferences on the recovery of the metal ions were investigated. A 5-ml portion of 0.4 M HCl solution was sufficient for quantitative elution of the metal ions from 0.5 ml of the sorbent packed in a 6.5 mm i.d. glass column. Quantitative recoveries were obtained in a pH range 5.5-6.5 for all the analytes. The volumes to be concentrated exceeding 500 ml, ionic strengths as high as 0.5 mol l-1, and acetate buffer concentrations up to 0.3 mol l-1 for Zn2+ and 0.4 mol l-1 for Cu2+ and Fe3+ did not have any significant effect on the recoveries. The system tolerated relatively high concentrations of diverse ions. Preconcentration factors up to 100 and detection limits of 0.31, 0.16 and 1.73 μg l-1 were obtained for Cu2+, Zn2+ and Fe3+, respectively, for their determination by a flame AAS instrument. The method was successfully applied to the metal ion determinations in several river water samples with good accuracy.

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