concanamycin-a and sodium-nitrate

concanamycin-a has been researched along with sodium-nitrate* in 1 studies

Other Studies

1 other study(ies) available for concanamycin-a and sodium-nitrate

ArticleYear
Is the Paracoccus halodenitrificans ATPase a chimeric enzyme?
    FEMS microbiology letters, 1996, Jun-15, Volume: 140, Issue:1

    Membranes from Paracoccus halodenitrificans contain an ATPase that is most active in the absence of NaCl. The most unusual characteristic of the enzyme is its pattern of sensitivity to various inhibitors. Azide and rhodamine 6G, inhibitors of F1F0-ATPases, inhibit ATP hydrolysis as do bafilomycin A1, concanamycin A (folimycin), N-ethylmaleimide, and p-chloromercuriphenylsulfonate which are inhibitors of vacuolar ATPases. This indiscriminate sensitivity suggests that this ATPase may be a hybrid and that caution should be exercised when using inhibition as a diagnostic for distinguishing between F1F0-ATPases and vacuolar ATPases.

    Topics: Adenosine Triphosphatases; Anti-Bacterial Agents; Azides; Dicyclohexylcarbodiimide; Enzyme Inhibitors; Ethylmaleimide; Macrolides; Membranes; Nitrates; Paracoccus; Potassium Chloride; Proton-Translocating ATPases; Rhodamines; Sodium Chloride; Vacuolar Proton-Translocating ATPases

1996