myxothiazol and tungstate

myxothiazol has been researched along with tungstate* in 2 studies

Other Studies

2 other study(ies) available for myxothiazol and tungstate

ArticleYear
Existence of aa3-type ubiquinol oxidase as a terminal oxidase in sulfite oxidation of Acidithiobacillus thiooxidans.
    Bioscience, biotechnology, and biochemistry, 2006, Volume: 70, Issue:7

    It was found that Acidithiobacillus thiooxidans has sulfite:ubiquinone oxidoreductase and ubiquinol oxidase activities in the cells. Ubiquinol oxidase was purified from plasma membranes of strain NB1-3 in a nearly homogeneous state. A purified enzyme showed absorption peaks at 419 and 595 nm in the oxidized form and at 442 and 605 nm in the reduced form. Pyridine ferrohaemochrome prepared from the enzyme showed an alpha-peak characteristic of haem a at 587 nm, indicating that the enzyme contains haem a as a component. The CO difference spectrum of ubiquinol oxidase showed two peaks at 428 nm and 595 nm, and a trough at 446 nm, suggesting the existence of an aa(3)-type cytochrome in the enzyme. Ubiquinol oxidase was composed of three subunits with apparent molecular masses of 57 kDa, 34 kDa, and 23 kDa. The optimum pH and temperature for ubiquinol oxidation were pH 6.0 and 30 degrees C. The activity was completely inhibited by sodium cyanide at 1.0 mM. In contrast, the activity was inhibited weakly by antimycin A(1) and myxothiazol, which are inhibitors of mitochondrial bc(1) complex. Quinone analog 2-heptyl-4-hydoroxyquinoline N-oxide (HOQNO) strongly inhibited ubiquinol oxidase activity. Nickel and tungstate (0.1 mM), which are used as a bacteriostatic agent for A. thiooxidans-dependent concrete corrosion, inhibited ubiquinol oxidase activity 100 and 70% respectively.

    Topics: Acidithiobacillus thiooxidans; Antimycin A; Cell Membrane; Electron Transport Complex IV; Heme; Hydrogen-Ion Concentration; Hydroxyquinolines; Methacrylates; Nickel; Oxidation-Reduction; Oxidoreductases; Protein Subunits; Sodium Cyanide; Sulfites; Thiazoles; Tungsten Compounds; Ubiquinone

2006
Mitochondrial electron transport as a source for nitric oxide in the unicellular green alga Chlorella sorokiniana.
    FEBS letters, 2004, Oct-08, Volume: 576, Issue:1-2

    Wild type (WT), and nitrate reductase (NR)- and nitrite-reductase (NiR)-deficient cells of Chlorella sorokiniana were used to characterize nitric oxide (NO) emission. The NO emission from nitrate-grown WT cells was very low in air, increased slightly after addition of nitrite (200 microM), but strongly under anoxia. Importantly, even completely NR-free mutants, as well as cells grown on tungstate, emitted NO when fed with nitrite under anoxia. Therefore, this NO production from nitrite was independent of NR and other molybdenum cofactor enzymes. Cyanide and inhibitors of mitochondrial complex III, myxothiazol or antimycin A, but not salicylhydroxamic acid (inhibitor of alternative oxidase) inhibited NO production by NR-free cells. In contrast, NiR-deficient cells growing on nitrate accumulated nitrite and emitted NO at very high equal rates in air and anoxia. This NO emission was 50% inhibited by salicylhydroxamic acid, indicating that in these cells the alternative oxidase pathway had been induced and reduced nitrite to NO.

    Topics: Antimycin A; Cell Hypoxia; Chlorella; Cyanides; Electron Transport Complex III; Enzyme Inhibitors; Kinetics; Methacrylates; Mitochondria; Mutation; Nitric Oxide; Nitrites; Salicylamides; Thiazoles; Tungsten Compounds

2004