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Journal of Bacteriology, November 1999, p. 6730-6738, Vol. 181, No. 21
Laboratoire d'Ecologie Microbienne du Sol,
CNRS-UMR 5557, l'Universite Claude-Bernard, 69622 Villeurbanne
Cedex, France,1 and Department of
Microbiology and Molecular Genetics, School of Medicine, Loma Linda
University, Loma Linda, California 923502
Received 26 April 1999/Accepted 23 August 1999
Laccase, a p-diphenol oxidase typical of plants and
fungi, has been found recently in a proteobacterium, Azospirillum
lipoferum. Laccase activity was detected in both a natural
isolate and an in vitro-obtained phase variant that originated from the
laccase-negative wild type. In this study, the electron transport
systems of the laccase-positive variant and its parental
laccase-negative forms were compared. During exponential (but not
stationary) growth under fully aerobic (but not under microaerobic)
conditions, the laccase-positive variant lost a respiratory branch that
is terminated in a cytochrome c oxidase of the
aa3 type; this was most likely due to a defect
in the biosynthesis of a heme component essential for the oxidase. The
laccase-positive variant was significantly less sensitive to the
inhibitory action of quinone analogs and fully resistant to inhibitors
of the bc1 complex, apparently due to the
rearrangements of its respiratory system. We propose that the loss of
the cytochrome c oxidase-containing branch in the variant
is an adaptive strategy to the presence of intracellular oxidized
quinones, the products of laccase activity.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Loss of Cytochrome c Oxidase Activity
and Acquisition of Resistance to Quinone Analogs in a
Laccase-Positive Variant of Azospirillum
lipoferum
*
Corresponding author. Mailing address: Department of
Microbiology and Molecular Genetics, School of Medicine, Loma Linda
University, Loma Linda, CA 92350. Phone: (909) 558-4480. Fax: (909)
558-4035. E-mail: izhulin{at}som.llu.edu.
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