Hemoglobin, nitric oxide and molecular mechanisms of hypoxic vasodilation.

Published

Journal Article (Review)

The protected transport of nitric oxide (NO) by hemoglobin (Hb) links the metabolic activity of working tissue to the regulation of its local blood supply through hypoxic vasodilation. This physiologic mechanism is allosterically coupled to the O(2) saturation of Hb and involves the covalent binding of NO to a cysteine residue in the beta-chain of Hb (Cys beta93) to form S-nitrosohemoglobin (SNO-Hb). Subsequent S-transnitrosation, the transfer of NO groups to thiols on the RBC membrane and then in the plasma, preserves NO vasodilator activity for delivery to the vascular endothelium. This SNO-Hb paradigm provides insight into the respiratory cycle and a new therapeutic focus for diseases involving abnormal microcirculatory perfusion. In addition, the formation of S-nitrosothiols in other proteins may regulate an array of physiological functions.

Full Text

Duke Authors

Cited Authors

  • Allen, BW; Stamler, JS; Piantadosi, CA

Published Date

  • October 2009

Published In

Volume / Issue

  • 15 / 10

Start / End Page

  • 452 - 460

PubMed ID

  • 19781996

Pubmed Central ID

  • 19781996

Electronic International Standard Serial Number (EISSN)

  • 1471-499X

Digital Object Identifier (DOI)

  • 10.1016/j.molmed.2009.08.002

Language

  • eng

Conference Location

  • England