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PvdP is a tyrosinase that drives maturation of the pyoverdine chromophore in Pseudomonas aeruginosa.


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.

SUBMITTER: Nadal-Jimenez P 

PROVIDER: S-EPMC4097581 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature

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PvdP is a tyrosinase that drives maturation of the pyoverdine chromophore in Pseudomonas aeruginosa.

Nadal-Jimenez Pol P   Koch Gudrun G   Reis Carlos R CR   Muntendam Remco R   Raj Hans H   Jeronimus-Stratingh C Margot CM   Cool Robbert H RH   Quax Wim J WJ  

Journal of bacteriology 20140509 14


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  ...[more]

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