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X-Ray Absorption Spectroscopy of Pseudomonas Cepacia Phthalate Dioxygenase

  • James E. Penner-Hahn
Part of the Basic Life Sciences book series (BLSC, volume 51)

Abstract

Bacterial degradation of aromatic compounds generally proceeds by a series of oxygenations. In Pseudomonas cepacia, the first step in phthalate metabolism is dihydroxylation to give phthalate 4,5-dihydrodiol. This reaction is catalyzed by a novel non-heme iron oxygenase. The phthalate dioxygenase from P. cepacia is a large (ca. 192,000 kDa) tetrameric protein containing one “Rieske-like” 2Fe/2S cluster and one mononuclear Fe site per monomer (Batie et al, 1987). We used x-ray absorption spectroscopy (XAS) to determine the structures of the metal sites in phthalate dioxygenase.

Keywords

Stanford Synchrotron Radiation Laboratory Rieske Cluster Mononuclear Site Phthalate Dioxygenase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1989

Authors and Affiliations

  • James E. Penner-Hahn
    • 1
  1. 1.Department of ChemistryUniversity of MichiganAnn ArborUSA

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