Atrazine chlorohydrolase from Pseudomonas sp. strain ADP is a metalloenzyme

Jennifer L. Seffernick, Hugh McTavish, Jeffrey P. Osborne, Mervyn L. De Souza, Michael J. Sadowsky, Lawrence P. Wackett

Research output: Contribution to journalArticlepeer-review

49 Scopus citations

Abstract

Atrazine chlorohydrolase (AtzA) from Pseudomonas sp. ADP initiates the metabolism of the herbicide atrazine by catalyzing a hydrolytic dechlorination reaction to produce hydroxyatrazine. Sequence analysis revealed AtzA to be homologous to metalloenzymes within the amidohydrolase protein superfamily. AtzA activity was experimentally shown to depend on an enzyme-bound, divalent transition-metal ion. Loss of activity obtained by incubating AtzA with the chelator 1,10-phenanthroline or oxalic acid was reversible upon addition of Fe(II), Mn(II), or Co(II) salts. Experimental evidence suggests a 1:1 metal to subunit stoichiometry, with the native metal being Fe(II). Our data show that the inhibitory effects of metals such as Zn(II) and Cu(II) are not the result of displacing the active site metal. Taken together, these data indicate that AtzA is a functional metalloenzyme, making this the first report, to our knowledge, of a metal-dependent dechlorinating enzyme that proceeds via a hydrolytic mechanism.

Original languageEnglish (US)
Pages (from-to)14430-14437
Number of pages8
JournalBiochemistry
Volume41
Issue number48
DOIs
StatePublished - Dec 3 2002

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