Reactions between nitric oxide and haemoglobin under physiological conditions

Andrew J. Gow, Jonathan S. Stamler

Research output: Contribution to journalArticlepeer-review

499 Citations (Scopus)


The tenet of high-affinity nitric oxide (NO) binding to a haemoglobin (Hb) has shaped our view of haem proteins and of small diffusible signaling molecules. Specifically, NO binds rapidly to haem iron in Hb (k ≃ 107 M- 1 s-1) (refs 1, 2) and once bound, the NO activity is largely irretrievable (K(d) ≃ 10-5 s-1) (refs 5-10); the binding is purportedly so fight as to be unaffected by O2 or CO. However, these general principles do not consider the allosteric state of Hb or the nature of the allosteric effector, and they mostly derive from the functional behaviour of fully nitrosylated Hb, whereas Hb is only partially nitrosylated in vivo. Here we show that oxygen drives the conversion of nitrosylhaemoglobin in the 'tense' T (or partially nitrosylated, deoxy) structure to S-nitrosohaemoglobin in the 'relaxed' R (or ligand-bound, oxy) structure. In the absence of oxygen, nitroxyl anion (NO-) is liberated in a reaction producing methaemoglobin. The yields of both S-nitrosohaemoglobin and methaemoglobin are dependent on the NO/Hb ratio. These newly discovered reactions elucidate mechanisms underlying NO function in the respiratory cycle, and provide insight into the aetiology of S-nitrosothiols, methaemoglobin and its related valency hybrids. Mechanistic reexamination of NO interactions with other haem proteins containing allosteric-site thiols may be warranted.

Original languageEnglish
Pages (from-to)169-173
Number of pages5
Issue number6663
Publication statusPublished - 8 Jan 1998
Externally publishedYes

ASJC Scopus subject areas

  • General

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