Blood flow regulation by S-nitrosohemoglobin in the physiological oxygen gradient.

Journal Article (Journal Article)

The binding of oxygen to heme irons in hemoglobin promotes the binding of nitric oxide (NO) to cysteinebeta93, forming S-nitrosohemoglobin. Deoxygenation is accompanied by an allosteric transition in S-nitrosohemoglobin [from the R (oxygenated) to the T (deoxygenated) structure] that releases the NO group. S-nitrosohemoglobin contracts blood vessels and decreases cerebral perfusion in the R structure and relaxes vessels to improve blood flow in the T structure. By thus sensing the physiological oxygen gradient in tissues, hemoglobin exploits conformation-associated changes in the position of cysteinebeta93 SNO to bring local blood flow into line with oxygen requirements.

Full Text

Duke Authors

Cited Authors

  • Stamler, JS; Jia, L; Eu, JP; McMahon, TJ; Demchenko, IT; Bonaventura, J; Gernert, K; Piantadosi, CA

Published Date

  • June 27, 1997

Published In

Volume / Issue

  • 276 / 5321

Start / End Page

  • 2034 - 2037

PubMed ID

  • 9197264

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.276.5321.2034


  • eng

Conference Location

  • United States