NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native Fe O Reaction.

The Rieske dioxygenases are a major subclass of mononuclear nonheme iron enzymes that play an important role in bioremediation. Recently, a high-spin Fe-(hydro)-peroxy intermediate (BZDOp) has been trapped in the peroxide shunt reaction of benzoate 1,2-dioxygenase. Defining the structure of this int...

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Publicado en:Journal of the American Chemical Society Vol. 140; no. 16; pp. 5544 - 5560
Autores principales: Sutherlin, Kyle D., Rivard, Brent S., Böttger, Lars H., Liu, Lei V., Rogers, Melanie S., Srnec, Martin, Kiyoung Park, Yoshitaka Yoda, Shinji Kitao, Yasuhiro Kobayashi, Makina Saito, Makoto Seto, Hu, Michael, Jiyong Zhao, Lipscomb, John D., Solomon, Edward I.
Formato: Artículo
Publicado: American Chemical Society 4/25/2018
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Acceso en línea:Ver este registro en EBSCOhost
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        10.1021/jacs.8b01822
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        atl: NRVS Studies of the Peroxide Shunt Intermediate in a Rieske Dioxygenase and Its Relation to the Native Fe O Reaction.
      aug:
        au:
          Sutherlin, Kyle D.
          Rivard, Brent S.
          Böttger, Lars H.
          Liu, Lei V.
          Rogers, Melanie S.
          Srnec, Martin
          Kiyoung Park
          Yoshitaka Yoda
          Shinji Kitao
          Yasuhiro Kobayashi
          Makina Saito
          Makoto Seto
          Hu, Michael
          Jiyong Zhao
          Lipscomb, John D.
          Solomon, Edward I.
        affil:
          Department of Chemistry, Stanford University, Stanford, California 94305, United States
          Department of Biochemistry, Molecular Biology, & Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, United States
          J. Heyrovský Institute of Physical Chemistry, The Czech Academy of Sciences, Dolejškova 2155/3, 182 23 Prague 8, Czech Republic
          Department of Chemistry, KAIST, Daejeon 34141, Republic of Korea
          Japan Synchrotron Radiation Research Institute, Hyogo 679-5198, Japan
          Research Reactor Institute, Kyoto University, Osaka 590-0494, Japan
          Advanced Photon Source, Argonne National Laboratory, Lemont, Illinois 60439, United States
          SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States
      su:
        Peroxides
        Dioxygenases
        Bioremediation
        Hydroperoxy radicals
        Benzoates
        Iron
        Density functional theory
      sug:
        subj:
          Peroxides
          Dioxygenases
          Bioremediation
          Hydroperoxy radicals
          Benzoates
          Iron
          Density functional theory
      ab: The Rieske dioxygenases are a major subclass of mononuclear nonheme iron enzymes that play an important role in bioremediation. Recently, a high-spin Fe-(hydro)-peroxy intermediate (BZDOp) has been trapped in the peroxide shunt reaction of benzoate 1,2-dioxygenase. Defining the structure of this intermediate is essential to understanding the reactivity of these enzymes. Nuclear resonance vibrational spectroscopy (NRVS) is a recently developed synchrotron technique that is ideal for obtaining vibrational, and thus structural, information on Fe sites, as it gives complete information on all vibrational normal modes containing Fe displacement. In this study, we present NRVS data on BZDOp and assign its structure using these data coupled to experimentally calibrated density functional theory calculations. From this NRVS structure, we define the mechanism for the peroxide shunt reaction. The relevance of the peroxide shunt to the native Fe/O reaction is evaluated. For the native Fe/O reaction, an Fe-superoxo intermediate is found to react directly with substrate. This process, while uphill thermodynamically, is found to be driven by the highly favorable thermodynamics of proton-coupled electron transfer with an electron provided by the Rieske [2Fe-2S] center at a later step in the reaction. These results offer important insight into the relative reactivities of Fe-superoxo and Fe-hydroperoxo species in nonheme Fe biochemistry.
      pubtype: Academic Journal
      doctype: Article
      src: R
    language: English
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