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Butyl isocyanide as a probe of the activation mechanism of soluble guanylate cyclase

Academic Article
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Overview

authors

  • Derbyshire, E. R.
  • Marletta, Michael

publication date

  • December 2007

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Nitric oxide (NO) is a physiologically relevant activator of the hemoprotein soluble guanylate cyclase (sGC). In the presence of NO, sGC is activated several hundredfold above the basal level by a mechanism that remains to be elucidated. The heme ligand n-butyl isocyanide (BIC) was used to probe the mechanism of NO activation of sGC. Electronic absorption spectroscopy was used to show that BIC binds to the sGC heme, forming a 6-coordinate complex with an absorbance maximum at 429 nm. BIC activates sGC 2-5-fold, and synergizes with the allosteric activator YC-1, to activate the enzyme 15-25-fold. YC-1 activates the sGC-BIC complex, and leads to an increase in both the V(max) and K(m). BIC was also used to probe the mechanism of NO activation. The activity of the sGC-BIC complex increases 15-fold in the presence of NO, without displacing BIC at the heme, which is consistent with previous reports that proposed the involvement of a non-heme NO binding site in the activation process.

subject areas

  • Animals
  • Binding Sites
  • Enzyme Activation
  • Guanylate Cyclase
  • Heme
  • Isocyanates
  • Ligands
  • Nitric Oxide
  • Spectroscopy, Electron Energy-Loss
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M705557200

PubMed ID

  • 17916555
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Additional Document Info

start page

  • 35741

end page

  • 35748

volume

  • 282

issue

  • 49

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