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4,4-difluorinated analogues of L-arginine and N(G)-hydroxy-L-arginine as mechanistic probes for nitric oxide synthase

Academic Article
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Overview

authors

  • Martin, N. I.
  • Woodward, J. J.
  • Winter, M. B.
  • Marletta, Michael

publication date

  • 2009

journal

  • Bioorganic & Medicinal Chemistry Letters  Journal

abstract

  • 4,4-Difluoro-l-arginine and 4,4-difluoro-N(G)-hydroxy-l-arginine were synthesized and shown to be substrates for the inducible isoform of nitric oxide synthase (iNOS). Binding of both fluorinated analogues to the NOS active site was also investigated using a spectral binding assay employing a heme domain construct of the inducible NOS isoform (iNOS(heme)). 4,4-Difluoro-N(G)-hydroxy-arginine was found to bind at the NOS active site in a unique manner consistent with a model involving ligation of the Fe(III) heme center by the oxygen atom of the N(G)-hydroxy moiety.

subject areas

  • Arginine
  • Catalysis
  • Chemistry, Pharmaceutical
  • Drug Design
  • Fluorine
  • Heme
  • Models, Chemical
  • Nitric Oxide Synthase
  • Oxygen
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Structure-Activity Relationship
  • Substrate Specificity
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Research

keywords

  • Fluorinated substrate analogues
  • Mechanistic probes
  • Nitric oxide synthase
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Identity

International Standard Serial Number (ISSN)

  • 0960-894X

Digital Object Identifier (DOI)

  • 10.1016/j.bmcl.2009.01.076

PubMed ID

  • 19230661
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Additional Document Info

start page

  • 1758

end page

  • 1762

volume

  • 19

issue

  • 6

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