Reeder, Brandon J (2010) The Redox Activity of Hemoglobins: From Physiologic Functions to Pathologic Mechanisms. Antioxidants & Redox Signaling, 13 (7). pp. 1087-1123. ISSN 1523-0864Full text not yet available from this repository.
Pentacoordinate respiratory hemoproteins such as hemoglobin and myoglobin have evolved to supply cells with oxygen. However, these respiratory heme proteins are also known to function as redox enzymes, reacting with compounds such as nitric oxide and peroxides. The recent discoveries of hexacoordinate hemoglobins in vertebrates and nonsymbiotic plants suggest that the redox activity of globins is inherent to the molecule. The uncontrolled formation of radical species resulting from such redox chemistry on respiratory hemoproteins can lead to oxidative damage and cellular toxicity. In this review, we examine the functions of various globins and the mechanisms by which these globins act as redox enzymes under physiologic conditions. Evidence that redox reactions also occur under disease conditions, leading to pathologic complications, also is examined, focusing on recent discoveries showing that the ferryl oxidation state of these hemoproteins is present in these disease states in vivo. In addition, we review the latest advances in the understanding of globin redox mechanisms and how they might affect cellular signaling pathways and how they might be controlled therapeutically or, in the case of hemoglobin-based blood substitutes, through rational design. Antioxid. Redox Signal. 13, 1087-1123.
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculty of Science and Engineering > Biological Sciences, School of|
|Depositing User:||Jim Jamieson|
|Date Deposited:||07 Oct 2011 10:55|
|Last Modified:||07 Oct 2011 10:55|
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