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Related Experiment Video

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A Tandem Liquid Chromatography–Mass Spectrometry-based Approach for Metabolite Analysis of Staphylococcus aureus
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Nitrate reductase system in Staphylococcus aureus wild type and mutants.

K A Burke, J Lascelles

    Journal of Bacteriology
    |July 1, 1975
    PubMed
    Summary

    Staphylococcus aureus respiratory nitrate reductase activity is induced by nitrate. This enzyme, primarily found in the cytoplasm when using benzyl viologen, shows unusual localization compared to other organisms.

    Area of Science:

    • Microbiology
    • Enzymology
    • Biochemistry

    Background:

    • Respiratory nitrate reductase is crucial for anaerobic respiration in many bacteria.
    • Staphylococcus aureus utilizes nitrate respiration, but the localization and regulation of its nitrate reductase are not fully understood.
    • Heme deficiency can impact bacterial respiratory enzyme function.

    Purpose of the Study:

    • To investigate the characteristics of respiratory nitrate reductase in Staphylococcus aureus.
    • To determine the cellular localization of nitrate reductase activity using different hydrogen donors.
    • To examine the effect of heme deficiency and specific inhibitors on enzyme activity and induction.

    Main Methods:

    • Studied nitrate reductase activity in wild-type and heme-deficient Staphylococcus aureus cells and spheroplast preparations.

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  • Assayed enzyme activity using lactate and reduced benzyl viologen as hydrogen donors.
  • Investigated enzyme induction, inhibition by specific chemicals (azide, cyanide, oxamate, etc.), and activation of an inactive form.

    • Main Results:

    • Nitrate reductase activity was rapidly induced by nitrate under non-aerobic conditions.
    • Lactate-dependent activity was primarily membrane-bound, while benzyl viologen-dependent activity was largely cytoplasmic.
    • Enzyme activity was inhibited by azide and cyanide; lactate-linked activity was sensitive to additional inhibitors. An inactive form induced by tungstate could be activated by molybdate.

    Conclusions:

    • Staphylococcus aureus respiratory nitrate reductase shares characteristics with enzymes from other organisms.
    • The predominant cytoplasmic localization of nitrate reductase activity, particularly with reduced benzyl viologen, is unusual.
    • Heme deficiency influences the proportion of cytoplasmic activity.