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Formation of active nitrite reductase (cytochromecd 1) in the strainParacoccus denitrificans HUUG25

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Abstract

Strain HUUG25 ofParacoccus denitrificans has been frequently thought to be devoid of allc-type cytochromes. We show here by means of enzymological and immunological techniques that the mutant synthesizes active nitrite reductase (cytochromecd 1) upon prolonged exposure to microoxic conditions. The synthesis occurred faster in the presence of exogenous hemin. The time pattern of 5-aminolevulinate synthase activity was also altered by the mutation. These findings suggest a defective regulation of heme supply to the site of nitrite reductase assembly in the periplasm.

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Authors and Affiliations

  1. Department of Biochemistry, Faculty of Science, Masaryk University, Kotlářská 2, CZ-61137, Brno, Czech Republic

    Ivana Mafchová & Igor Kučera

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  1. Ivana Mafchová
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  2. Igor Kučera
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Correspondence to Igor Kučera.

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Mafchová, I., Kučera, I. Formation of active nitrite reductase (cytochromecd 1) in the strainParacoccus denitrificans HUUG25. Arch. Microbiol. 164, 58–62 (1995). https://doi.org/10.1007/BF02568735

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  • DOI: https://doi.org/10.1007/BF02568735

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