S-Nitrosohemoglobin: an allosteric mediator of NO group function in mammalian vasculature.
Since the discovery of NO as the endothelium-derived relaxing factor, there has been considerable interest in how NO interacts with hemoglobin (Hb). Numerous investigations have highlighted the possibility that rather than operating as a sink to consume NO, the vasculature can operate as a delivery mechanism for NO. The principal hypothesis proposed to explain this phenomenon is that Hb can transport NO on the conserved cysteine residue beta93 and deliver that NO to the tissues in an allosterically dependent manner. This proposal has been termed the S-Nitrosohemoglobin (SNO-Hb) Hypothesis. This review addresses the experimental evidence that led to development of this hypothesis and examines much of the research that resulted from its generation. Specifically it covers the evidence concerning NO in the vasculature, the SNO-Hb Hypothesis itself, the biochemical and biophysical data relating to NO and Hb interactions, SNO-Hb in human physiology, and alternative vascular forms of NO. Finally a model of NO in the vasculature in which SNO-Hb forms the central core is proposed.
Frehm
Eric J
EJ
Children's Hospital of Philadelphia, Division of Neonatology, Department of Pediatrics, University of Pennsylvania, Philadelphia, PA 19104, USA.
Bonaventura
Joseph
J
Gow
Andrew J
AJ
D000495:Allosteric Site; D000818:Animals; D001692:Biological Transport; D003545:Cysteine / Q000737:chemistry; D004730:Endothelium, Vascular / Q000473:pathology; D006418:Heme / Q000737:chemistry; D006454:Hemoglobins / Q000737:chemistry* / Q000502:physiology; D006801:Humans; D008954:Models, Biological; D009569:Nitric Oxide / Q000737:chemistry* / Q000378:metabolism
D006454:Hemoglobins; C103574:S-nitrosohemoglobin; D009569:Nitric Oxide; D006418:Heme; D003545:Cysteine