title: 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.
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands Instituto Gulbenkian de Ciência, Oeiras, Portugal.
authors.forename: Pol
authors.initials: P
authors.lastname: Nadal-Jimenez
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands Research Center for Infectious Diseases ZINF, Würzburg Universität, Josef-Schneider-Strasse 2, Würzburg, Germany.
authors.forename: Gudrun
authors.initials: G
authors.lastname: Koch
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands Department of Cell Biology, UT Southwestern Medical Center, Dallas, Texas, USA.
authors.forename: Carlos R
authors.initials: CR
authors.lastname: Reis
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands.
authors.forename: Remco
authors.initials: R
authors.lastname: Muntendam
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands.
authors.forename: Hans
authors.initials: H
authors.lastname: Raj
authors.affiliation: Mass Spectrometry Core Facility, University of Groningen, A. Deusinglaan, Groningen, The Netherlands.
authors.forename: C Margot
authors.initials: CM
authors.lastname: Jeronimus-Stratingh
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands.
authors.forename: Robbert H
authors.initials: RH
authors.lastname: Cool
authors.affiliation: Department of Pharmaceutical Biology, University of Groningen, Antonius Deusinglaan, Groningen, The Netherlands w.j.quax@rug.nl.
authors.forename: Wim J
authors.initials: WJ
authors.lastname: Quax
mesh_terms: D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D020134:Catalytic Domain; D015964:Gene Expression Regulation, Bacterial / Q000502:physiology; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology*; D008958:Models, Molecular; D014442:Monophenol Monooxygenase / Q000235:genetics / Q000378:metabolism*; D009842:Oligopeptides / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D011487:Protein Conformation; D021381:Protein Transport; D011550:Pseudomonas aeruginosa / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D009842:Oligopeptides; C042453:pyoverdin; D014442:Monophenol Monooxygenase