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

doi:10.1007/s12104-016-9707-6

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

Surgery

Research output: Contribution to journal › Article › peer-review

5 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	395-400
Number of pages	6
Journal	Biomolecular NMR Assignments
Volume	10
Issue number	2
DOIs	https://doi.org/10.1007/s12104-016-9707-6
State	Published - Oct 1 2016

Keywords

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

ASJC Scopus subject areas

Structural Biology
Biochemistry

Access to Document

10.1007/s12104-016-9707-6

Cite this

@article{f0841fef5c014276a5466524d43fb65c,

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

abstract = "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.",

keywords = "H-NOX, NMR spectroscopy, Nitric oxide binding domain, Recombinant protein expression, Soluble guanylyl cyclase, sGC",

author = "Alexandropoulos, \{Ioannis I.\} and Argyriou, \{Aikaterini I.\} and Marousis, \{Kostas D.\} and Stavros Topouzis and Andreas Papapetropoulos and Spyroulias, \{Georgios A.\}",

note = "Publisher Copyright: {\textcopyright} 2016, Springer Science+Business Media Dordrecht.",

year = "2016",

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doi = "10.1007/s12104-016-9707-6",

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T1 - 1H, 13C, 15N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the heme–nitric oxide/oxygen binding (H-NOX) domain

AU - Alexandropoulos, Ioannis I.

AU - Argyriou, Aikaterini I.

AU - Marousis, Kostas D.

AU - Topouzis, Stavros

AU - Papapetropoulos, Andreas

AU - Spyroulias, Georgios A.

PY - 2016/10/1

Y1 - 2016/10/1

N2 - 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.

AB - 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.

KW - H-NOX

KW - NMR spectroscopy

KW - Nitric oxide binding domain

KW - Recombinant protein expression

KW - Soluble guanylyl cyclase

KW - sGC

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DO - 10.1007/s12104-016-9707-6

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