PvdP Is a Tyrosinase That Drives Maturation of the Pyoverdine Chromophore in Pseudomonas aeruginosa

Pol Nadal-Jimenez, Gudrun Koch, Carlos R. Reis, Remco Muntendam, Hans Raj, C. Margot Jeronimus-Stratingh, Robbert H. Cool, Wim J. Quax*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

24 Citations (Scopus)

Abstract

The iron binding siderophore pyoverdine constitutes a major adaptive factor contributing to both virulence and survival in fluorescent pseudomonads. For decades, pyoverdine production has allowed the identification and classification of fluorescent and nonfluorescent pseudomonads. Here, we demonstrate that PvdP, a periplasmic enzyme of previously unknown function, is a tyrosinase required for the maturation of the pyoverdine chromophore in Pseudomonas aeruginosa. PvdP converts the nonfluorescent ferribactin, containing two iron binding groups, into a fluorescent pyoverdine, forming a strong hexadentate complex with ferrous iron, by three consecutive oxidation steps. PvdP represents the first characterized member of a small family of tyrosinases present in fluorescent pseudomonads that are required for siderophore maturation and are capable of acting on large peptidic substrates.

Original languageEnglish
Pages (from-to)2681-2690
Number of pages10
JournalJournal of Bacteriology
Volume196
Issue number14
DOIs
Publication statusPublished - Jul-2014

Keywords

  • BACTERIAL TYROSINASES
  • IRON TRANSPORT
  • SIDEROPHORES
  • BIOSYNTHESIS
  • IDENTIFICATION
  • FLUORESCENT
  • ACQUISITION
  • ALIGNMENTS
  • PRECURSORS
  • SECRETION

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