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- W1996331410 abstract "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.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.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.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." @default.
- W1996331410 created "2016-06-24" @default.
- W1996331410 creator A5013490785 @default.
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- W1996331410 creator A5060269662 @default.
- W1996331410 creator A5076405771 @default.
- W1996331410 creator A5078640285 @default.
- W1996331410 date "2013-06-10" @default.
- W1996331410 modified "2023-09-30" @default.
- W1996331410 title "Molecular Controls of the Oxygenation and Redox Reactions of Hemoglobin" @default.
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