1H, 13C, 15N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the heme–nitric oxide/oxygen binding (H-NOX) domain

Ioannis I. Alexandropoulos, Aikaterini I. Argyriou, Kostas D. Marousis, Stavros Topouzis, Andreas Papapetropoulos, Georgios A. Spyroulias

Research output: Contribution to journalArticle

1 Scopus citations


The H-NOX (Heme-nitric oxide/oxygen binding) domain is conserved across eukaryotes and bacteria. In human soluble guanylyl cyclase (sGC) the H-NOX domain functions as a sensor for the gaseous signaling agent nitric oxide (NO). sGC contains the heme-binding H-NOX domain at its N-terminus, which regulates the catalytic site contained within the C-terminal end of the enzyme catalyzing the conversion of GTP (guanosine 5′-triphosphate) to GMP (guanylyl monophosphate). Here, we present the backbone and side-chain assignments of the 1H, 13C and 15N resonances of the 183-residue H-NOX domain from Nostoc sp. through solution NMR.

Original languageEnglish (US)
Pages (from-to)395-400
Number of pages6
JournalBiomolecular NMR Assignments
Issue number2
StatePublished - Oct 1 2016
Externally publishedYes



  • H-NOX
  • Nitric oxide binding domain
  • NMR spectroscopy
  • Recombinant protein expression
  • sGC
  • Soluble guanylyl cyclase

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry

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