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

DOI Web Site 被引用文献9件
  • Seungil Han
    S. Han, S. W. Muchmore, J. T. Bolin, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.
  • Lindsay D. Eltis
    L. D. Eltis, Department of Biochemistry, Université Laval, Ste. Foy, Quebec G1K 7P4, Canada.
  • Kenneth N. Timmis
    K. N. Timmis, Bereich Mikrobiologie, Gesellschaft für Biotechnologische Forschung mbH, Mascheroder Weg 1, D-38124 Braunschweig, Germany.
  • Steven W. Muchmore
    S. Han, S. W. Muchmore, J. T. Bolin, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.
  • Jeffrey T. Bolin
    S. Han, S. W. Muchmore, J. T. Bolin, Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-1392, USA.

書誌事項

公開日
1995-11-10
DOI
  • 10.1126/science.270.5238.976
公開者
American Association for the Advancement of Science (AAAS)

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説明

<jats:p> 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 <jats:italic>Pseudomonas cepacia</jats:italic> 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. </jats:p>

収録刊行物

  • Science

    Science 270 (5238), 976-980, 1995-11-10

    American Association for the Advancement of Science (AAAS)

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