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The Cytochrome C Maturation Operon Is Involved In Manganese Oxidation In Pseudomonas Putida GB-1

J. P. M. de Vrind, G. J. Brouwers, P. L. A. M. Corstjens, J. den Dulk, E. W. de Vrind-de Jong

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ABSTRACT A Pseudomonas putida strain, strain GB-1, oxidizes Mn 2+ 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 (Tn 5 ) mutagenesis several classes of mutants with differences in Mn 2+ oxidation and/or secretion of the Mn 2+ -oxidizing activity were identified. Preliminary analysis of the Tn 5 insertion site in one of the nonoxidizing mutants suggested that a multicopper oxidase-related enzyme is involved in Mn 2+ oxidation. The insertion site in another mutant was preliminarily identified as a gene involved in the general protein secretion pathway. Two mutants defective in Mn 2+ -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 Tn 5 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 Mn 2+ oxidation in P. putida GB-1. A possible relationship between porphyrin secretion resulting from the ccm mutation and stimulation of pyoverdine production is discussed.