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Binding modes for the first coupled electron and proton addition to FeMoco of nitrogenase

Academic Article
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Overview

authors

  • Lovell, T.
  • Li, J.
  • Case, David A.
  • Noodleman, Louis

publication date

  • May 2002

journal

  • Journal of the American Chemical Society  Journal

abstract

  • A combined broken-symmetry density functional and electrostatics approach has been used to model the one-electron reduced and protonated state of the iron-molybdenum cofactor active site of nitrogenase. The active site of the protein contains Fe, Mo, S, N, and O atoms, and many possible sites for protonation have been examined. A novel hydridic proton asymmetrically located in the central cavity created by six Fe sites is most favored from the calculations. Under physiological turnover conditions of low electron flux, the formation of this iron-hydride intermediate may represent a first step towards cofactor liberation of dihydrogen in the absence of dinitrogen.

subject areas

  • Binding Sites
  • Electrons
  • Iron
  • Molybdenum
  • Molybdoferredoxin
  • Nitrogenase
  • Protons
  • Thermodynamics
  • Tricarboxylic Acids
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Identity

International Standard Serial Number (ISSN)

  • 0002-7863

Digital Object Identifier (DOI)

  • 10.1021/ja012311v

PubMed ID

  • 11971686
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Additional Document Info

start page

  • 4546

end page

  • 4547

volume

  • 124

issue

  • 17

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