The University of Southampton
University of Southampton Institutional Repository

Biochemical characterization of S-nitrosohemoglobin. Mechanisms underlying synthesis, no release, and biological activity

Wolzt, Michael, MacAllister, Raymond J., Davis, Dana, Feelisch, Martin, Moncada, Salvador, Vallance, Patrick and Hobbs, Adrian J. (1999) Biochemical characterization of S-nitrosohemoglobin. Mechanisms underlying synthesis, no release, and biological activity The Journal of Biological Chemistry, 274, (41), pp. 28983-28990. (doi:10.1074/jbc.274.41.28983). (PMID:10506146).

Record type: Article


S-Nitrosohemoglobin (SNO-Hb) has been suggested to act as an endogenous NO donor and physiological regulator of blood pressure. However, the mechanisms responsible for the formation of SNO-Hb and those underlying the release of NO and subsequent biological activity have yet to be elucidated. In the present study, a number of nitrosated oxyhemoglobin (HbO(2)) derivatives have been synthesized and characterized. HbO(2) can be nitrosated at up to three distinct residues, one in the alpha-globin chain and two in the beta-chain. A beta-chain mononitrosated species (designated "SNO-Hb"), generated by the reaction of HbO(2) and S-nitrosoglutathione, released NO via a thiol-dependent mechanism involving nucleophilic attack at the nitrosated thiol functionality of SNO-Hb; in the case of glutathione, this process was associated with the formation of a mixed disulfide. In contrast, multinitrosated hemoglobin species released NO and relaxed vascular smooth muscle by a thiol-independent mechanism. HbO(2) scavenged potently NO released from SNO-Hb and inhibited its vasorelaxant properties. These data show that the predominant vasoactive species released from SNO-Hb is NO, with HNO a putative intermediate; the presence of a low molecular weight thiol is a prerequisite for this process. Such observations have important implications for the generation, metabolic fate, and biological activity of S-nitrosothiols.

Full text not available from this repository.

More information

Published date: 8 October 1999
Organisations: Clinical & Experimental Sciences


Local EPrints ID: 337880
ISSN: 0021-9258
PURE UUID: 37eb1ee9-249a-4ab3-8e82-7db6574dac72
ORCID for Martin Feelisch: ORCID iD

Catalogue record

Date deposited: 29 Jun 2012 11:06
Last modified: 18 Jul 2017 06:00

Export record



Author: Michael Wolzt
Author: Raymond J. MacAllister
Author: Dana Davis
Author: Martin Feelisch ORCID iD
Author: Salvador Moncada
Author: Patrick Vallance
Author: Adrian J. Hobbs

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton:

ePrints Soton supports OAI 2.0 with a base URL of

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.