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A study on nitrate reductase from Propionibacterium acidi-propionici.

M Kaneko, M Ishimoto

    Journal of Biochemistry
    |January 1, 1978
    PubMed
    Summary
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    Propionibacterium acidi-propionici nitrate reductase (NaR) efficiently reduces nitrate using various substrates. This enzyme, likely a molybdo-protein, is partially inhibited by oxygen and fumarate.

    Area of Science:

    • Microbiology
    • Enzymology
    • Biochemistry

    Background:

    • Nitrate reductase (NaR) plays a crucial role in microbial metabolism.
    • Understanding NaR from Propionibacterium acidi-propionici can reveal insights into bacterial anaerobic respiration.

    Purpose of the Study:

    • To characterize the nitrate reductase (NaR) from Propionibacterium acidi-propionici.
    • To investigate the enzyme's catalytic properties, substrate specificity, and potential prosthetic groups.

    Main Methods:

    • Enzyme extraction and partial purification using Emulgen 810 and multiple chromatographic techniques (DEAE-cellulose, Sepharose 4B, DEAE-Sephadex).
    • Enzyme activity assays with various electron donors (glycerol phosphate, NADH, lactate, viologens) and acceptors (nitrate, chlorate).
    • Determination of molecular weight (Sepharose 4B gel filtration), isoelectric point, pH optimum, and kinetic parameters (Km for nitrate).

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  • Inhibition studies using fumarate, oxygen, azide, cyanide, and thiocyanate.
  • Investigation of enzyme regulation using tungstate and molybdate during cell growth.

    • Main Results:

    • Cell extracts exhibited high NaR activity, utilizing glycerol phosphate, NADH, or lactate as electron donors.
    • The enzyme was purified 46-fold and found to be particulate, requiring detergent for solubilization and glycerol for stabilization.
    • Key properties include a molecular weight of ~230,000 Da, pI of 5.0-5.5, pH optimum of 6.5-7.5, and Km for nitrate of 0.1 mM.
    • Methyl and benzyl viologens were effective electron donors, while FAD and FMN were not. Chlorate served as an alternative electron acceptor.
    • Activity was partially inhibited by fumarate and oxygen, and strongly inhibited by azide, cyanide, and thiocyanate.
    • Tungstate in the growth medium reduced NaR levels, with partial restoration by molybdate, suggesting NaR is a molybdo-protein.

    Conclusions:

    • The nitrate reductase from Propionibacterium acidi-propionici is a particulate molybdo-protein with specific substrate preferences and regulatory characteristics.
    • Its properties are similar to NaR enzymes found in other bacterial species, highlighting conserved biochemical mechanisms.
    • Further characterization could elucidate its precise role in the bacterium's energy metabolism and electron transport pathways.