Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions.

Wallace, William J.; Houtchens, Robert A.; Maxwell, John C.; Caughey, Winslow S.

doi:10.1016/s0021-9258(18)34620-9

Cited by 237 publications

(77 citation statements)

References 43 publications

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“…P450), 9 d whereas the protonation at the proximal oxygen has been often shown to liberate protonated superoxide, as in the case of unproductive degradation of oxyhemoglobin to met-hemoglobin. 13 …”

Section: Introductionmentioning

confidence: 99%

Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study

et al. 2021

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Section: Introductionmentioning

confidence: 99%

Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study

et al. 2021

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“…It is well known that auto-oxidation of hemoglobin takes place under in-vivo conditions to generate met-hemoglobin [Fe(III)], peroxide, and superoxide radicals, collectively known as reactive oxygen species (ROS) [12][13][14]. Under normal conditions a certain basal level of hemoglobin oxidation and corresponding level of ROS is always present in RBCs [15].…”

Section: Introductionmentioning

confidence: 99%

Erythroid spectrin binding modulates peroxidase and catalase activity of heme proteins

Bose

Aggarwal

Das

et al. 2021

Preprint

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Hemoglobin oxidation due to oxidative stress and disease conditions leads to generation of ROS (reactive oxygen species) and membrane attachment of hemoglobin in-vivo, where its redox activity leads to peroxidative damage of membrane lipids and proteins. Spectrin, the major component of the RBC membrane skeleton, is known to interact with hemoglobin and, here this interaction is shown to increase hemoglobin peroxidase activity in the presence of reducing substrate ABTS (2, 2-Azino-Bis-3-Ethylbenzothiazoline-6-Sulfonic Acid). It is also shown that in the absence of reducing substrate, spectrin forms covalently cross-linked aggregates with hemoglobin which display no peroxidase activity. This may have implications in the clearance of ROS and limiting peroxidative damage. Spectrin is found to modulate the peroxidase activity of different hemoglobin variants like A, E, and S, and of isolated globin chains from each of these variants. This may be of importance in disease states like sickle cell disease and HbE-β-thalassemia, where increased oxidative damage and free globin subunits are present due to the defects inherent in the hemoglobin variants associated with these diseases. This hypothesis is corroborated by lipid peroxidation experiments. The modulatory role of spectrin is shown to extend to other heme proteins, namely catalase and cytochrome-c. Experiments with free heme and Raman spectroscopy of heme proteins in the presence of spectrin show that structural alterations occur in the heme moiety of the heme proteins on spectrin binding, which may be the structural basis of increased enzyme activity.

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“…Thus, the inability of an organism to capture and deliver oxygen to cells leads to the loss of the organism's capacity to obtain energy from consumed foods which can halt the metabolism and in severe cases, could lead to death of the organism (Onwubiko et al, 2000). Cell asphyxiation could occur when the capacity of the haemoglobin to deliver oxygen to cells is reduced via the process of oxidation of the haem-bound ferrous iron at the ligand binding site (Wallace et al, 1982).…”

Section: Introductionmentioning

confidence: 99%

Haemoglobin Oxidation: A possible mechanism of crude oil toxicity in fish

2016

Int. J. Biosci.

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Haemoglobin oxidation occurs in erythrocytes. It involves the loss of an electron from the ferrous (Fe 2+ ) ion to the ferric (Fe 3+ ) state in the presence of an oxidant. Crude oil, which contains polycyclic aromatic hydrocarbons (PAHs), has the capacity of serving as oxidants to fish haemoglobin to yield the methaemoglobin (Fe 3+ ) species which has lost the capacity to bind oxygen. This study reveals that various quantities (20, 60, 100 and 200 µl) of crude oil used to contaminate and incubate fish haemoglobin at 25 ºC increased the methaemoglobin absorbance at 630 nm wavelength due to methaemoglobin (Fe 3+ ) while there was a decrease at 540 nm and 577 nm. Since polycyclic aromatic hydrocarbons (with alkylated side chains) are the only component in crude oil that is absorbed by fish, it is suggestive that these compounds may be responsible for haemoglobin oxidation in fish.

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Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions.

Cited by 237 publications

References 43 publications

Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study

Proton-coupled electron transfer reactivities of electronically divergent heme superoxide intermediates: a kinetic, thermodynamic, and theoretical study

Erythroid spectrin binding modulates peroxidase and catalase activity of heme proteins

Haemoglobin Oxidation: A possible mechanism of crude oil toxicity in fish

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