Medical College of Wisconsin
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S-nitrosohemoglobin: a biochemical perspective. Free Radic Biol Med 2004 Apr 15;36(8):947-58

Date

04/03/2004

Pubmed ID

15059635

DOI

10.1016/j.freeradbiomed.2004.01.008

Scopus ID

2-s2.0-1642588213 (requires institutional sign-in at Scopus site)   29 Citations

Abstract

It has been suggested that S-nitrosohemoglobin (HbSNO) is an oxygen-dependent mediator of nitric oxide delivery to vascular smooth muscle cells, thus regulating vascular tone and blood flow. Central to this much-debated hypothesis is the concept that our previous understanding of the interaction between nitric oxide and ferrous hemoglobin was deficient. In this review we will examine the chemical and biochemical mechanisms for the formation of HbSNO, the properties of HbSNO, and the release of nitric oxide from HbSNO. This review concludes that although novel reactions of nitric oxide, nitrite, and S-nitrosothiols with hemoglobin have been uncovered, there is little evidence to support the notion that the interaction of nitric oxide with ferrous hemoglobin is more complex than had been previously established.

Author List

Zhang Y, Hogg N

Author

Neil Hogg PhD Senior Associate Dean, Professor in the Biophysics department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Free Radicals
Heme
Hemoglobins
Humans
Models, Biological
Models, Chemical
Models, Molecular
Nitric Oxide
Nitrites
Oxidation-Reduction
Oxygen