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Science 10 November 1995:
Vol. 270. no. 5238, pp. 976 - 980
DOI: 10.1126/science.270.5238.976
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Reports

Crystal Structure of the Biphenyl-Cleaving Extradiol Dioxygenase from a PCB-Degrading Pseudomonad

Seungil Han,  Lindsay D. Eltis,  Kenneth N. Timmis,  Steven W. Muchmore (1),  Jeffrey T. Bolin (2)

Polychlorinated biphenyls (PCBs) typify a class of stable aromatic pollutants that are targeted by bioremediation strategies. In the aerobic degradation of biphenyl by bacteria, the key step of ring cleavage is catalyzed by an Fe(II)-dependent extradiol dioxygenase. The crystal structure of 2,3-dihydroxybiphenyl 1,2-dioxygenase from a PCB-degrading strain of Pseudomonas cepacia has been determined at 1.9 angstrom resolution. The monomer comprises amino- and carboxyl-terminal domains. Structural homology between and within the domains reveals evolutionary relationships within the extradiol dioxygenase family. The iron atom has five ligands in square pyramidal geometry: one glutamate and two histidine side chains, and two water molecules.


S. Han, S. W. Muchmore, J. T. Bolin, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.
L. D. Eltis, Department of Biochemistry, Université Laval, Ste. Foy, Quebec G1K 7P4, Canada.
K. N. Timmis, Bereich Mikrobiologie, Gesellschaft für Biotechnologische Forschung mbH, Mascheroder Weg 1, D-38124 Braunschweig, Germany.
(1) Present address: Abbott Laboratories, Department 42T Building AP9A, 100 Abbott Park Road, Abbott Park, IL 60064-3500, USA.
(2) To whom correspondence should be addressed.


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