Document Detail


Molecular controls of the oxygenation and redox reactions of hemoglobin.
MedLine Citation:
PMID:  23198874     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
SIGNIFICANCE: 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.
Authors:
Celia Bonaventura; Robert Henkens; Abdu I Alayash; Sambuddha Banerjee; Alvin L Crumbliss
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Review     Date:  2013-01-21
Journal Detail:
Title:  Antioxidants & redox signaling     Volume:  18     ISSN:  1557-7716     ISO Abbreviation:  Antioxid. Redox Signal.     Publication Date:  2013 Jun 
Date Detail:
Created Date:  2013-04-29     Completed Date:  2013-10-30     Revised Date:  2013-11-06    
Medline Journal Info:
Nlm Unique ID:  100888899     Medline TA:  Antioxid Redox Signal     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2298-313     Citation Subset:  IM    
Affiliation:
Nicholas School of the Environment, Duke University Marine Laboratory, Beaufort, NC 28516, USA. bona@duke.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Blood Substitutes / chemistry,  metabolism
Hemoglobins / chemistry,  genetics*,  metabolism*
Humans
Oxidation-Reduction
Oxygen / blood
Oxygen Consumption*
Protein Binding
Chemical
Reg. No./Substance:
0/Blood Substitutes; 0/Hemoglobins; 7782-44-7/Oxygen

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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