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The menaquinol oxidase of Bacillus subtilis W23

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Abstract

The quinol oxidase appears to be mainly responsible for the oxidation of bacterial MKH2 in Bacillus subtilis W23 growing with either glucose or succinate. The activity of the enzyme was maximum with dimethylnaphthoquinol, a water-soluble analogue of the bacterial menaquinol. Menadiol or duroquinol were less actively respired, and naphthoquinol was not oxidized at all. After fourtyfold purification the isolated enzyme contained 5.3 μmol cytochrome aa 3 per gram of protein and negligible amounts of cytochrome b and c. The turnover number based on cytochrome aa 3 was about 103 electrons · s-1 at pH 7 and 37°C. The preparation consisted mainly of a M r 57000 and a M r 36000 polypeptide. The N-terminal amino acid sequence of the latter polypeptide differed from that predicted by the qoxA gene of B. subtilis strain 168 (Santana et al. 1992), in that asp-14 predicted by qoxA was missing in the M r 36000 polypeptide.

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Abbreviations

DMN:

2,3-dimethyl-1,4-naphthoquinone

DMNH2 :

2,3-dimethyl-1,4-naphthoquinol

Duroquinol:

2,3,5,6-tetramethyl-1,4-benzoquinol

MK:

menaquinone

MKH2 :

menaquinol

NBH2 :

2,3-dimethoxy-5-methyl-6-(n-nonyl)-1,4-benzoquinol

TMPD:

N,N,N′, N′,-tetramethyl-1,4-phenylenediamine

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Authors and Affiliations

  1. Institut für Mikrobiologie, J.-W.-Goethe Universität, Theodor-Stern-Kai 7, Haus 75A, W-6000, Frankfurt am Main, Germany

    E. Lemma & A. Kröger

  2. Zehtrum der Biologischen Chemie, Klinikum der J.-W.-Goethe Universität, W-6000, Frankfurt am Main, Germany

    H. Schägger

Authors
  1. E. Lemma
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  2. H. Schägger
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  3. A. Kröger
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Lemma, E., Schägger, H. & Kröger, A. The menaquinol oxidase of Bacillus subtilis W23. Arch. Microbiol. 159, 574–578 (1993). https://doi.org/10.1007/BF00249037

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