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.
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© 1989 Plenum Press, New York
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Penner-Hahn, J.E. (1989). X-Ray Absorption Spectroscopy of Pseudomonas Cepacia Phthalate Dioxygenase. In: Sweet, R.M., Woodhead, A.D. (eds) Synchrotron Radiation in Structural Biology. Basic Life Sciences, vol 51. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8041-2_20
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DOI: https://doi.org/10.1007/978-1-4684-8041-2_20
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