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Properties and function of clostridial membrane ATPase.

V Riebeling, K Jungermann

    Biochimica Et Biophysica Acta
    |June 8, 1976
    PubMed
    Summary

    This study identified ATPase in Clostridium pasteurianum membranes, revealing its Mg2+-dependent activity and sensitivity to DCCD. The findings suggest this ATPase functions in proton translocation, a phylogenetically ancient process in prokaryotes.

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    Area of Science:

    • Biochemistry
    • Microbiology
    • Molecular Biology

    Background:

    • ATPase (ATP phosphohydrolase, EC 3.6.1.3) is crucial for cellular energy metabolism.
    • Understanding bacterial ATPases provides insights into fundamental biological processes and evolutionary history.

    Purpose of the Study:

    • To characterize the ATPase activity in the strict anaerobic bacterium Clostridium pasteurianum.
    • To investigate the properties and function of the membrane-bound ATPase in C. pasteurianum.

    Main Methods:

    • Detection and partial purification of ATPase from C. pasteurianum membrane fractions.
    • Enzyme activity assays with various substrates, metal ions, and inhibitors.
    • Comparison of membrane-bound and solubilized ATPase properties.

    Main Results:

    • Approximately 70% of ATPase activity was membrane-associated and Mg2+-dependent.
    • The membrane-bound ATPase was sensitive to dicyclohexylcarbodiimide (DCCD) but not oligomycin, ouabain, or NaN3.
    • Solubilization of the enzyme led to instability and altered properties.

    Conclusions:

    • The C. pasteurianum ATPase likely functions in proton translocation, similar to mitochondrial ATPases.
    • Prokaryotic ATPases are ancient, potentially evolving into ATP-forming enzymes in aerobic organisms.

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