Molecular controls of the oxygenation and redox reactions of hemoglobin.

Journal Article (Review;Journal Article)


The broad classes of O(2)-binding proteins known as hemoglobins (Hbs) carry out oxygenation and redox functions that allow organisms with significantly different physiological demands to exist in a wide range of environments. This is aided by allosteric controls that modulate the protein's redox reactions as well as its O(2)-binding functions.

Recent advances

The controls of Hb's redox reactions can differ appreciably from the molecular controls for Hb oxygenation and come into play in elegant mechanisms for dealing with nitrosative stress, in the malarial resistance conferred by sickle cell Hb, and in the as-yet unsuccessful designs for safe and effective blood substitutes.

Critical issues

An important basic principle in consideration of Hb's redox reactions is the distinction between kinetic and thermodynamic reaction control. Clarification of these modes of control is critical to gaining an increased understanding of Hb-mediated oxidative processes and oxidative toxicity in vivo.

Future directions

This review addresses emerging concepts and some unresolved questions regarding the interplay between the oxygenation and oxidation reactions of structurally diverse Hbs, both within red blood cells and under acellular conditions. Developing methods that control Hb-mediated oxidative toxicity will be critical to the future development of Hb-based blood substitutes.

Full Text

Duke Authors

Cited Authors

  • Bonaventura, C; Henkens, R; Alayash, AI; Banerjee, S; Crumbliss, AL

Published Date

  • June 2013

Published In

Volume / Issue

  • 18 / 17

Start / End Page

  • 2298 - 2313

PubMed ID

  • 23198874

Pubmed Central ID

  • PMC4047995

Electronic International Standard Serial Number (EISSN)

  • 1557-7716

International Standard Serial Number (ISSN)

  • 1523-0864

Digital Object Identifier (DOI)

  • 10.1089/ars.2012.4947


  • eng