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Determination of the Proton Environment of High Stability Menasemiquinone Intermediate in Escherichia coli Nitrate Reductase A by Pulsed EPR

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اقرأ أكثر حفظ في قائمتي
  • معلومة اضافية
    • Contributors:
      Institut de Microbiologie de la Méditerranée (IMM); Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS); Institut für Metallkunde und Metallphysik (IMM); RWTH Aachen University = Rheinisch-Westfälische Technische Hochschule Aachen (RWTH Aachen); CNRS, the Agence Nationale de la Recherche, and Aix-Marseille Universite´.
    • بيانات النشر:
      HAL CCSD
      American Society for Biochemistry and Molecular Biology
    • الموضوع:
      2012
    • Collection:
      Aix-Marseille Université: HAL
    • نبذة مختصرة :
      International audience ; Background: Escherichia coli nitrate reductase A highly stabilizes a semiquinone catalytic intermediate. Results: Three proton hyperfine couplings to this radical with atypical characteristics are characterized. Conclusion: Semiquinone binding is strongly asymmetric and occurs via a single short in-plane H-bond. Significance: Learning how the protein environment tunes the semiquinone properties is crucial for understanding the quinol utilization mechanism by energy-transducing enzymes.
    • الرقم المعرف:
      10.1074/jbc.M111.325100
    • الدخول الالكتروني :
      https://hal.science/hal-03248799
      https://hal.science/hal-03248799v1/document
      https://hal.science/hal-03248799v1/file/zbc4662.pdf
      https://doi.org/10.1074/jbc.M111.325100
    • Rights:
      info:eu-repo/semantics/OpenAccess
    • الرقم المعرف:
      edsbas.E5E348EE