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A new decoration for nitric oxide synthase - a zn(cys)4 site

Academic Article
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Overview

authors

  • Ludwig, M. L.
  • Marletta, Michael

publication date

  • April 1999

journal

  • Structure with Folding & Design  Journal

abstract

  • Intense interest in the action and synthesis of nitric oxide has fueled structural studies of nitric oxide synthase (NOS). The monomeric and dimeric heme domains of inducible NOS were the first NOS structures to be described. A recent independent analysis of the corresponding heme domains from endothelial NOS confirms most of the features found earlier and also reveals a novel Zn(Cys)4 center - a new feature for NOS.

subject areas

  • Animals
  • Arginine
  • Binding Sites
  • Biopterin
  • Citrulline
  • Cysteine
  • Dimerization
  • Electron Transport
  • Macromolecular Substances
  • Models, Molecular
  • NADP
  • Nitric Oxide
  • Nitric Oxide Synthase
  • Oxidation-Reduction
  • Protein Conformation
  • Zinc
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Identity

International Standard Serial Number (ISSN)

  • 0969-2126

Digital Object Identifier (DOI)

  • 10.1016/s0969-2126(99)80047-1

PubMed ID

  • 10198293
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Additional Document Info

start page

  • R73

end page

  • R79

volume

  • 7

issue

  • 4

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