Residues stabilizing the heme moiety of the nitric oxide sensor soluble guanylate cyclase

Peter M. Schmidt, Christiane Rothkegel, Frank Wunder, Henning Schröder, Johannes Peter Stasch

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Soluble guanylate cyclase, a heterodimer consisting of an α- and a heme-containing β-subunit, is the major receptor for the biological messenger nitric oxide (NO) and is involved in various signal transduction pathways. The heme moiety of the enzyme is bound between the axial heme ligand histidine105 and the recently identified counterparts of the heme propionic acids, tyrosine135 and arginine139. The latter residues together with an invariant serine137 form the unique heme binding motif Y-x-S-x-R. In this work, we show that replacement of the serine137 with alanine destabilizes the binding of the heme moiety and impairs NO-mediated soluble guanylate cyclase activation.

Original languageEnglish (US)
Pages (from-to)67-74
Number of pages8
JournalEuropean Journal of Pharmacology
Issue number1-2
StatePublished - Apr 18 2005

Bibliographical note

Copyright 2008 Elsevier B.V., All rights reserved.


  • BAY 41-2272
  • BAY 58-2667
  • Heme
  • Nitric oxide
  • Soluble guanylate cyclase
  • YC-1
  • cGMP


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