Impaired maturation of the siderophore pyoverdine chromophore in Pseudomonas fluorescens ATCC 17400 deficient for the cytochrome c biogenesis protein CcmC

FEBS Lett. 2002 Jul 17;523(1-3):23-8. doi: 10.1016/s0014-5793(02)02915-0.

Abstract

Pyoverdines are the main siderophores of fluorescent pseudomonads. They comprise a quinoline chromophore, a peptide chain, and a dicarboxylic acid or a dicarboxylic acid amide side chain. Each Pseudomonas species produces a pyoverdine with a different peptide chain. A cytochrome c biogenesis DeltaccmC mutant of Pseudomonas fluorescens ATCC 17400 produces multiple pyoverdine forms, showing differences at the level of the chromophore or the side chain. When grown in the presence of L-cysteine, DeltaccmC produces only ferribactin, a non-fluorescent precursor of pyoverdine, while addition of oxidized glutathione improves pyoverdine production. We suggest that the conversion of ferribactin to pyoverdine does not take place in the DeltaccmC mutant because of lack of oxidizing power in the periplasm.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins*
  • Cysteine / metabolism
  • Glutathione Disulfide / metabolism
  • Membrane Proteins / deficiency
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Mutation
  • Oligopeptides*
  • Periplasm / metabolism
  • Pigments, Biological / isolation & purification
  • Pigments, Biological / metabolism*
  • Pseudomonas fluorescens / metabolism*
  • Siderophores / isolation & purification
  • Siderophores / metabolism

Substances

  • Bacterial Proteins
  • CcmC protein, bacteria
  • Membrane Proteins
  • Oligopeptides
  • Pigments, Biological
  • Siderophores
  • pyoverdin
  • Cysteine
  • Glutathione Disulfide