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Nitric oxide binding to prokaryotic homologs of the soluble guanylate cyclase beta 1 h-nox domain

Academic Article
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Overview

authors

  • Boon, E. M.
  • Davis, J. H.
  • Tran, R.
  • Karow, D. S.
  • Huang, S. H.
  • Pan, D. H.
  • Miazgowicz, M. M.
  • Mathies, R. A.
  • Marletta, Michael

publication date

  • 2006

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The heme cofactor in soluble guanylate cyclase (sGC) is a selective receptor for NO, an important signaling molecule in eukaryotes. The sGC heme domain has been localized to the N-terminal 194 amino acids of the beta1 subunit of sGC and is a member of a family of conserved hemoproteins, called the H-NOX family (Heme-Nitric Oxide and/or OXygen-binding domain). Three new members of this family have now been cloned and characterized, two proteins from Legionella pneumophila (L1 H-NOX and L2 H-NOX) and one from Nostoc punctiforme (Np H-NOX). Like sGC, L1 H-NOX forms a 5-coordinate Fe(II)-NO complex. However, both L2 H-NOX and Np H-NOX form temperature-dependent mixtures of 5- and 6-coordinate Fe(II)-NO complexes; at low temperature, they are primarily 6-coordinate, and at high temperature, the equilibrium is shifted toward a 5-coordinate geometry. This equilibrium is fully reversible with temperature in the absence of free NO. This process is analyzed in terms of a thermally labile proximal Fe(II)-His bond and suggests that in both the 5- and 6-coordinate Fe(II)-NO complexes of L2 H-NOX and Np H-NOX, NO is bound in the distal heme pocket of the H-NOX fold. NO dissociation kinetics for L1 H-NOX and L2 H-NOX have been determined and support a model in which NO dissociates from the distal side of the heme in both 5- and 6-coordinate complexes.

subject areas

  • Binding Sites
  • Guanylate Cyclase
  • Heme
  • Kinetics
  • Legionella pneumophila
  • Nitric Oxide
  • Nostoc
  • Solubility
  • Temperature
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M600557200

PubMed ID

  • 16728401
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Additional Document Info

start page

  • 21892

end page

  • 21902

volume

  • 281

issue

  • 31

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