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J. Biol. Chem., Vol. 260, Issue 27, 14633-14635, Nov, 1985

Crystallographic characterization of phthalate oxygenase reductase, an iron-sulfur flavoprotein from Pseudomonas cepacia

CC Correll, CJ Batie, DP Ballou and ML Ludwig

Pseudomonads grown on phthalate synthesize a series of enzymes that metabolize this aromatic substrate. Among the inducible enzymes is a reductase which transfers electrons from NADH to the terminal dioxygenase that converts phthalate to the corresponding cis-1,2- dihydrodiol (Keyser, P. (1976) Ph. D. thesis, University of Miami; Ribbons, D. W., and Evans, W. C. (1960) Biochem. J. 76, 310-318). The phthalate oxygenase reductase induced in Pseudomonas cepacia is a single polypeptide chain (Mr approximately equal to 33,000) with two prosthetic groups, FMN and [2Fe-2S]. This oxidoreductase has been crystallized at pH 6.7 from polyethylene glycol 6000 in space group R3 with a = b = 113.4 A and c = 77.7 A (hexagonal indexing).
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				C. Correll, C. Batie, D. Ballou, and M. Ludwig Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S] Science, December 4, 1992; 258(5088): 1604 - 1610. [Abstract] [PDF]