Phthalate Dioxygenase Reductase: a Modular Structure for Electron Transfer from Pyridine Nucleotides to [2Fe-2S]

DOI Web Site 被引用文献6件
  • Carl C. Correll
    Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor, MI 48109.
  • Christopher J. Batie
    Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor, MI 48109.
  • David P. Ballou
    Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor, MI 48109.
  • Martha L. Ludwig
    Department of Biological Chemistry and Biophysics, University of Michigan, Ann Arbor, MI 48109.

抄録

<jats:p> Phthalate dioxygenase reductase (PDR) is a prototypical iron-sulfur flavoprotein (36 kilodaltons) that utilizes flavin mononucleotide (FMN) to mediate electron transfer from the two-electron donor, reduced nicotinamide adenine nucleotide (NADH), to the one-electron acceptor, [2Fe-2S]. The crystal structure of oxidized PDR from <jats:italic>Pseudomonas cepacia</jats:italic> has been analyzed at 2.0 angstrom resolution resolution; reduced PDR and pyridine nucleotide complexes have been analyzed at 2.7 angstrom resolution. NADH, FMN, and the [2Fe-2S] cluster, bound to distinct domains, are brought together near a central cleft in the molecule, with only 4.9 angstroms separating the flavin 8-methyl and a cysteine sulfur ligated to iron. The domains that bind FMN and [2Fe-2S] are packed so that the flavin ring and the plane of the [2Fe-2S] core are approximately perpendicular. The [2Fe-2S] group is bound by four cysteines in a site resembling that in plant ferredoxins, but its redox potential (-174 millivolts at pH 7.0) is much higher than the potentials of plant ferredoxins. Structural and sequence similarities assign PDR to a distinct family of flavoprotein reductases, all related to ferredoxin NADP <jats:sup>+</jats:sup> -reductase. </jats:p>

収録刊行物

  • Science

    Science 258 (5088), 1604-1610, 1992-12-04

    American Association for the Advancement of Science (AAAS)

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