Hemoglobin Autooxidation/Oxidation Mechanisms and Methemoglobin Prevention or Reduction Processes in the Bloodstream Literature review and outline of autooxidation reaction

Faivre, B.; Menu, Patrick; Labrude, Pierre; Vigneron, C.

doi:10.3109/10731199809118943

Cited by 95 publications

(83 citation statements)

References 37 publications

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“…both pH-and temperature dependence (10,40,64,111,120,121). Examination of Hb autoxidation rates (using both ''bench-top'' and in vivo assays) has revealed that the rate of the transition from ferrous to ferric Hb depends on several factors, including the O 2 pressure, temperature, integrity of the red blood cells, and levels of intracellular reductants and anionic effectors.…”

Section: Autoxidationmentioning

confidence: 99%

Molecular Controls of the Oxygenation and Redox Reactions of Hemoglobin

Bonaventura

Henkens

Alayash

et al. 2013

Antioxidants & Redox Signaling

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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 Hbmediated oxidative toxicity will be critical to the future development of Hb-based blood substitutes. Antioxid. Redox Signal. 18, 2298-2313. General PrinciplesEmergence of proteins capable of transporting O 2 I n this review, we examine the adaptive changes in the molecular controls of hemoglobin (Hb) oxygenation and oxidation that have evolved to meet the highly varied physiological and environmental demands of respiring organisms. Globins came into being during the planet's long early period of anoxia/hypoxia, and recent studies show that globins are either expressed or inducible in almost all cells (98). Studies have shown that one evolutionary pathway of Hb is that of a multipurpose domain attached to a variety of unrelated proteins, thus forming molecules with different functions (126). This pathway has allowed structurally distinct Hbs to evolve: (i) to protect against the high levels of nitrosative stress of the earth's early environment; (ii) to protect against O 2 -linked oxidation; (iii) to act as O 2 sensors that help regulate the expression of proteins during periods of hypoxia or anoxia; and (iv) to enable aerobic respiration by facilitating diffusion and/or acting as O 2 carriers (44,56,57,70,71,73,107). A common theme in the fascinating story of Hb evolution is the emergence of distinct mechanisms for controlling Hb's oxygenation and redox functions.Since increased amounts of O 2 were released in our planet's early history, O 2 toxicity brought about species extinction on a global scale. On the other hand, this ''oxygen pollution'' made possible a new biological process, that of aerobic respiration. A tremendous gain in the energy obtainable from oxidation of energy-rich metabolites was achieved when organisms evolve...

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Section: Autoxidationmentioning

confidence: 99%

Molecular Controls of the Oxygenation and Redox Reactions of Hemoglobin

Bonaventura

Henkens

Alayash

et al. 2013

Antioxidants & Redox Signaling

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“…ferrous (Fe 2+ ) Hb binding oxygen (O 2 ), is known to undergo spontaneous intramolecular oxidationreduction reactions, in which the iron is oxidized to the ferric (Fe 3+ ) form (metHb) and the oxygen is reduced to superoxide. Further reactions lead to formation of ferryl (Fe 4+ ) Hb, free heme and various ROS [6]. ROS include hydrogen peroxide and the free radicals superoxide and hydroxyl radicals.…”

Section: Introductionmentioning

confidence: 99%

Increased levels of cell-free hemoglobin, oxidation markers, and the antioxidative heme scavenger α1-microglobulin in preeclampsia

Olsson

Centlow

Rutardóttir

et al. 2010

Free Radical Biology and Medicine

102

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Preeclampsia is a major cause of morbidity and mortality during pregnancy. To date, the pathogenesis of the disease is not fully understood. Recent studies show that preeclampsia is associated with overexpression of hemoglobin genes α2 and γ and accumulation of the protein in the vascular lumen of the placenta. Hypothesizing that cell-free hemoglobin leaks from the placenta into the maternal circulation and contributes to the endothelial damage and symptoms by inducing oxidative stress, we analysed fetal and adult hemoglobin (HbF, HbA), haptoglobin, oxidation markers and the heme scavenger and antioxidant α 1 -microglobulin in plasma, urine and placenta in preeclamptic women (n=28) and normal pregnancies (n=27).The mean plasma concentrations of HbF, HbA, protein carbonyl groups, membrane peroxidation capacity and α 1 -microglobulin were significantly increased in preeclamptic women. The levels of total plasma Hb correlated strongly with the systolic blood pressure.The plasma haptoglobin concentrations of women with preeclampsia were significantly depressed. Increased amounts of α 1 -microglobulin-mRNA and protein were found in placenta from preeclamptic women and the levels of plasma and placenta α 1 -microglobulin correlated to plasma Hb-concentrations. The heme-degrading form t-α 1 -microglobulin was significantly increased in urine in preeclampsia. These results support that hemoglobin-induced oxidative stress is a pathogenic factor in preeclampsia.

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“…Further downstream reactions lead to formation of ferryl (Fe 4+ ) hemoglobin, free heme and various reactive oxygen species (ROS) [2]. ROS include hydrogen peroxide and the free radicals superoxide and hydroxyl radicals.…”

Section: Introductionmentioning

confidence: 99%