ubiquinone and potassium-cyanate

ubiquinone has been researched along with potassium-cyanate* in 2 studies

Other Studies

2 other study(ies) available for ubiquinone and potassium-cyanate

Article	Year
Ubiquinol:cytochrome c oxidoreductase (complex III). Effect of inhibitors on cytochrome b reduction in submitochondrial particles and the role of ubiquinone in complex III. The Journal of biological chemistry, 2001, Jun-01, Volume: 276, Issue:22 Two sets of studies have been reported on the electron transfer pathway of complex III in bovine heart submitochondrial particles (SMP). 1) In the presence of myxothiazol, MOA-stilbene, stigmatellin, or of antimycin added to SMP pretreated with ascorbate and KCN to reduce the high potential components (iron-sulfur protein (ISP) and cytochrome c(1)) of complex III, addition of succinate reduced heme b(H) followed by a slow and partial reduction of heme b(L). Similar results were obtained when SMP were treated only with KCN or NaN(3), reagents that inhibit cytochrome oxidase, not complex III. The average initial rate of b(H) reduction under these conditions was about 25-30% of the rate of b reduction by succinate in antimycin-treated SMP, where both b(H) and b(L) were concomitantly reduced. These results have been discussed in relation to the Q-cycle hypothesis and the effect of the redox state of ISP/c(1) on cytochrome b reduction by succinate. 2) Reverse electron transfer from ISP reduced with ascorbate plus phenazine methosulfate to cytochrome b was studied in SMP, ubiquinone (Q)-depleted SMP containing Topics: Animals; Anti-Bacterial Agents; Antimycin A; Ascorbic Acid; Cattle; Cyanates; Cytochrome b Group; Cytochrome c Group; Electron Transport Complex III; Electrons; Enzyme Inhibitors; Heme; Methylphenazonium Methosulfate; Mitochondria; Models, Biological; Myocardium; Oxidation-Reduction; Succinic Acid; Time Factors; Ubiquinone	2001
Effect of physiological electron donors and acceptors on F1-ATPase. Revista espanola de fisiologia, 1981, Volume: 37, Issue:3 The hydrolytic activity of F1-ATPase isolated from rat liver was enhanced in the presence of NADH, FADH2, QH2 or reduced cyt c. The extent of this activation depended largely on substrate concentration. F1-ATPase sensitivity to bicarbonate or dinitrophenol activators decreased in the presence of any of those electron donors, which originated as well a slight sensitivity to oligomycin and a sensitivity increase to the inhibitory anion OCN-. In the presence of oxidized carriers the sensitivity to bicarbonate, dinitrophenol, or OCN- was not modified, and the enzyme remained oligomycin insensitive. Topics: Adenosine Triphosphatases; Animals; Cyanates; Cytochrome c Group; Dinitrophenols; Enzyme Activation; Flavin-Adenine Dinucleotide; Mitochondria, Liver; NAD; Oligomycins; Proton-Translocating ATPases; Rats; Ubiquinone	1981

Article

Year

Ubiquinol:cytochrome c oxidoreductase (complex III). Effect of inhibitors on cytochrome b reduction in submitochondrial particles and the role of ubiquinone in complex III.

The Journal of biological chemistry, 2001, Jun-01, Volume: 276, Issue:22

Two sets of studies have been reported on the electron transfer pathway of complex III in bovine heart submitochondrial particles (SMP). 1) In the presence of myxothiazol, MOA-stilbene, stigmatellin, or of antimycin added to SMP pretreated with ascorbate and KCN to reduce the high potential components (iron-sulfur protein (ISP) and cytochrome c(1)) of complex III, addition of succinate reduced heme b(H) followed by a slow and partial reduction of heme b(L). Similar results were obtained when SMP were treated only with KCN or NaN(3), reagents that inhibit cytochrome oxidase, not complex III. The average initial rate of b(H) reduction under these conditions was about 25-30% of the rate of b reduction by succinate in antimycin-treated SMP, where both b(H) and b(L) were concomitantly reduced. These results have been discussed in relation to the Q-cycle hypothesis and the effect of the redox state of ISP/c(1) on cytochrome b reduction by succinate. 2) Reverse electron transfer from ISP reduced with ascorbate plus phenazine methosulfate to cytochrome b was studied in SMP, ubiquinone (Q)-depleted SMP containing

Topics: Animals; Anti-Bacterial Agents; Antimycin A; Ascorbic Acid; Cattle; Cyanates; Cytochrome b Group; Cytochrome c Group; Electron Transport Complex III; Electrons; Enzyme Inhibitors; Heme; Methylphenazonium Methosulfate; Mitochondria; Models, Biological; Myocardium; Oxidation-Reduction; Succinic Acid; Time Factors; Ubiquinone

2001

Effect of physiological electron donors and acceptors on F1-ATPase.

Revista espanola de fisiologia, 1981, Volume: 37, Issue:3

The hydrolytic activity of F1-ATPase isolated from rat liver was enhanced in the presence of NADH, FADH2, QH2 or reduced cyt c. The extent of this activation depended largely on substrate concentration. F1-ATPase sensitivity to bicarbonate or dinitrophenol activators decreased in the presence of any of those electron donors, which originated as well a slight sensitivity to oligomycin and a sensitivity increase to the inhibitory anion OCN-. In the presence of oxidized carriers the sensitivity to bicarbonate, dinitrophenol, or OCN- was not modified, and the enzyme remained oligomycin insensitive.

Topics: Adenosine Triphosphatases; Animals; Cyanates; Cytochrome c Group; Dinitrophenols; Enzyme Activation; Flavin-Adenine Dinucleotide; Mitochondria, Liver; NAD; Oligomycins; Proton-Translocating ATPases; Rats; Ubiquinone

1981