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Applied and Environmental Microbiology, October 1998, p. 3556-3562, Vol. 64, No. 10
Leiden Institute of Chemistry, Gorlaeus
Laboratories, Leiden University, 2300 RA Leiden, The Netherlands
Received 23 April 1998/Accepted 1 July 1998
A Pseudomonas putida strain, strain GB-1, oxidizes
Mn2+ to Mn oxide in the early stationary growth phase. It
also secretes a siderophore (identified as pyoverdine) when it is
subjected to iron limitation. After transposon (Tn5)
mutagenesis several classes of mutants with differences in
Mn2+ oxidation and/or secretion of the
Mn2+-oxidizing activity were identified. Preliminary
analysis of the Tn5 insertion site in one of the
nonoxidizing mutants suggested that a multicopper oxidase-related
enzyme is involved in Mn2+ oxidation. The insertion site in
another mutant was preliminarily identified as a gene involved in the
general protein secretion pathway. Two mutants defective in
Mn2+-oxidizing activity also secreted porphyrins into the
medium and appeared to be derepressed for pyoverdine production. These
strains were chosen for detailed analysis. Both mutants were shown to contain Tn5 insertions in the ccmF gene, which
is part of the cytochrome c maturation operon. They were
cytochrome oxidase negative and did not contain c-type
cytochromes. Complementation with part of the ccm operon
isolated from the wild type restored the phenotype of the parent
strain. These results indicate that a functional ccm operon
is required for Mn2+ oxidation in P. putida
GB-1. A possible relationship between porphyrin secretion resulting
from the ccm mutation and stimulation of pyoverdine
production is discussed.
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
The Cytochrome c Maturation Operon Is
Involved in Manganese Oxidation in Pseudomonas putida
GB-1
*
Corresponding author. Mailing address: Leiden Institute
of Chemistry, Gorlaeus Laboratories, Leiden University, P.O. Box 9502, 2300 RA Leiden, The Netherlands. Phone: (31)71-5274707. Fax:
(31)71-5274340. E-mail: vrind_j{at}chem.leidenuniv.nl.
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