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.

The interaction between phosphoryl transferase and submitochondrial particles

1968 ◽  
Vol 46 (7) ◽  
pp. 677-683 ◽  
Author(s):  
Robert E. Beyer
Keyword(s):  
Adenine Nucleotide ◽  
Major Determinant ◽  
Phosphoryl Group ◽  
Antimycin A ◽  
Submitochondrial Particles ◽  
Phosphorylated Form ◽  
Mitochondrial Transfer ◽  
Probable Role ◽  
Phosphoryl Groups

The interaction between purified phosphoryl transferase and submitochondrial particles has been studied. In the presence of submitochondrial particles the transferase is phosphorylated and the phosphorylated form of the transferase is dephosphorylated. Both of these interactions require that the particle be actively carrying out oxidation of succinate or NADH. Both antimycin A and oligomycin suppress the phosphorylation and dephosphorylation reactions. The uncoupler p-trifluoromethoxy-carbonylcyanide phenylhydrazone prevents the particle-mediated phosphorylation of the transferase but stimulates the dephosphorylation of the phosphorylated transferase to a slight extent. The concentration of bound adenine nucleotide in the particles appears to be a major determinant of the rate of phosphorylation of the transferase, and this dependence is consistent with the fact that the transfer of a phosphoryl group from the phosphorylated transferase to ADP proceeds rapidly and spontaneously. The probable role of the transferase in the mitochondrial transfer of phosphoryl groups from endogenous ATP to exogenous ADP is evaluated.

Lipid peroxidation by bovine heart submitochondrial particles stimulated by 1,1′-dimethyl-4,4′-bipyridylium dichloride (paraquat)

1983 ◽  
Vol 32 (1) ◽  
pp. 13-19 ◽  
Author(s):  
Takeyoshi Sata ◽  
Koichiro Takeshige ◽  
Ryoichi Takayanagi ◽  
Shigeki Minakami
Keyword(s):  
Lipid Peroxidation ◽  
Submitochondrial Particles ◽  
Bovine Heart

scholarly journals Low-level chemiluminescence of bovine heart submitochondrial particles

1980 ◽  
Vol 186 (3) ◽  
pp. 659-667 ◽  
Author(s):  
Enrique Cadenas ◽  
Alberto Boveris ◽  
Britton Chance
Keyword(s):  
Lipid Peroxidation ◽  
Cytochrome C ◽  
Light Emission ◽  
Cumene Hydroperoxide ◽  
Radical Reactions ◽  
Submitochondrial Particles ◽  
Butyl Hydroperoxide ◽  
Low Level ◽  
Bovine Heart ◽  
Β Carotene

Submitochondrial particles from bovine heart mitochondria showed low-level chemiluminescence when supplemented with organic hydroperoxides. Chemiluminescence seems to measure integratively radical reactions involved in lipid peroxidation and related processes. Maximal light-emission was about 1500 counts/s and was reached 2–10min after addition of hydroperoxides. Ethyl hydroperoxide, cumene hydroperoxide and t-butyl hydroperoxide were effective in that order. Antimycin and rotenone increased chemiluminescence by 50–60%; addition of substrates, NADH and succinate did not produce marked changes in the observed chemiluminescence. Cyanide inhibited chemiluminescence; half-maximal inhibitory effect was obtained with 0.03mm-cyanide and the inhibition was competitive with respect to t-butyl hydroperoxide. Externally added cytochrome c (10–20μm) had a marked stimulatory effect on chemiluminescence, namely a 12-fold increase in light-emission of antimycin-inhibited submitochondrial particles. Stimulation of hydroperoxide-induced chemiluminescence of submitochondrial particles by cytochrome c was matched by a burst of O2 consumption. O2 is believed to participate in the chain radical reactions that lead to lipid peroxidation. Superoxide anion seems to be involved in the chemiluminescence reactions as long as light-emission was 50–60% inhibitible by superoxide dismutase. Singlet-oxygen quenchers, e.g. β-carotene and 1,4-diazabicyclo[2,2,2]-octane, affected light-emission. β-Carotene was effective either when incorporated into the membranes or added to the cuvette. The present paper suggests that singlet molecular oxygen is mainly responsible for the light-emission in the hydroperoxide-supplemented submitochondrial particles.

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 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 Alteration of inner-membrane components and damage to electron-transfer activities of bovine heart submitochondrial particles induced by NADPH-dependent lipid peroxidation

1982 ◽  
Vol 202 (1) ◽  
pp. 97-105 ◽  
Author(s):  
H Narabayashi ◽  
K Takeshige ◽  
S Minakami
Keyword(s):  
Lipid Peroxidation ◽  
Electron Transfer ◽  
Cytochrome C ◽  
Succinate Dehydrogenase ◽  
Sodium Dodecyl ◽  
Submitochondrial Particles ◽  
Inner Membrane ◽  
Cytochrome C Reductase ◽  
Bovine Heart ◽  
Membrane Components

We investigated the changes of the inner-membrane components and the electron-transfer activities of bovine heart submitochondrial particles induced by the lipid peroxidation supported by NADPH in the presence of ADP-Fe3+. Most of the polyunsaturated fatty acids were lost as a result of the peroxidation, and phospholipids were changed to polar species. Ubiquinone was also modified to polar substances as the peroxidation proceeded. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis showed the disappearance of 27000-Mr and 30000-Mr proteins and the appearance of highly polymerized substances. Flavins and cytochromes were not diminished, but the respiratory activity was lost. The reactions of NADH oxidase and NADH-cytochrome c reductase were most sensitive to the peroxidation, followed by those of succinate oxidase and succinate-cytochrome c reductase. Succinate dehydrogenase and duroquinol-cytochrome c reductase were inactivated by more extensive peroxidation, but cytochrome c oxidase was only partially inactivated. NADH-ferricyanide reductase was not inactivated. The pattern of the inactivation indicated that the lipid peroxidation affected the electron transport intensively between NADH dehydrogenase and ubiquinone, and moderately at the succinate dehydrogenase step and between ubiquinone and cytochrome c.

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