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

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Research Paper 01/07/2016
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Haemoglobin Oxidation: A possible mechanism of crude oil toxicity in fish

B. A. Ezeawgula , H. A. Onwubiko
Int. J. Biosci.9( 1), 25-33, July 2016.
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Haemoglobin oxidation occurs in erythrocytes. It involves the loss of an electron from the ferrous (Fe2+) ion to the ferric (Fe3+) 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 (Fe3+) 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 (Fe3+) 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.


Billiard S, Querbach K, Hodson P. 1999. Toxicity of retene to early life stages of two fresh water fish species. Environmental Toxicology and Chemistry 18(9), 2070-2077. http://dx.doi.org/10.1002/etc.5620180927

Boyiri T, Safo MK, Danso-Danguah RE, Kister J, Poyart C, Abraham DJ. 1995. Bisaldehyde allosteric effectors as molecular ratchets and probes. Biochemistry 34 (46), 15021-15036. www.ncbi.nlm.nih.gov/pubmed/7578115

Brunori M, Falcioni G, Fioretti E, Guardino B, Rolilio TG. 1975. Formation of superoxide in the autooxidation of isolated alpha and beta chains of human haemoglobin and its involvement in hemichrome precipitation. European Journal of Biochemistry 53(1), 99-104. http://onlinelibrary.wiley.com/doi/10.1111/j.1432103 3.1975.tb04046.x/epdf

Carls MG, Holland L, Larsen M, Collier TK, Scholz NL, Incardona JP. 2008. Fish embryos are damaged by dissolved PAHs, not oil particles. Aquatic Toxicology 88(2), 121-127. http://dx.doi.org/10.1016/j.aquatox.2008.03.014

Ekweozor IK. 1989. A review of the effects of oil pollution in West African environment. Discovery and Innovation 1(3), 27-37.

Hall FG, Gray IE. 1929. The haemoglobin concentration of the blood of marine fishes. Journal of Biological Chemistry 81(3), 589-594. http://www.jbc.org/content/81/3/589.full.pdf

Jacob HS, Winterhalter KH. 1970. The role of hemoglobin heme loss in Heinz body formation: studies with a partially heme-deficient hemoglobin and with genetically unstable hemoglobins. The Journal of Clinical Investigation 49(11), 2008-2016. http://dx.doi.org/10.1172/jci106421

Jaffe ER, Neumann G. 1964. A comparison of the effect of menadione, methylene blue and ascorbic acid on the reduction of methaemoglobin in vivo. Nature (London) 202, 607-608. http://dx.doi.org/10.1038/202607a0

Jarolim P, Lahav M, Liu SC, Palek J. 1990. Effect of haemoglobin oxidation products on the stability of red cell membrane skeletons and the associations of skeletal proteins: Correlation with a release of hemin. Blood 76(10), 2125-2131. www.ncbi.nlm.nih.gov/pubmed/2242431

Misra HP, Fridovich I. 1972. The generation of superoxide radical during autoxidation of haemoglobin. The Journal of Biological Chemistry 247(21), 6960-6962. http://www.jbc.org/content/247/21/6960

Onwubiko HA, Hazzard JA, Noble RW, Caughey WS. 1982. Demonstration of inositol hexaphosphate induced changes at the ligand binding site of carphaemoglobin carbonyl. Biochemical and Biophysical Research Communications 106(1), 223-227. http://ac.els-cdn.com/0006291X82920812/1-s2.0-0006291X82920812-main.pdf

Onwubiko  HA,  Onwubiko  GN,  Nwosu  MO. 2000. Haemoglobin oxidation as a mechanism of toxicity by extracts of tephrosia vogelii hook in the African catfish (Clarias gariepenus). Journal of Pharmaceutical Research and Development 5(1), 51-59.

Perutz MF. 1979. Regulation of oxygen affinity of haemoglobin: Influence of the structure of the globin on the haem iron. Annual Review of Biochemistry 48, 327-386.

Reza DM, Akbar MA, Parviz N, Ghourchian, Hadeyat-Olah, Shahrokh S. 2002. Inhibition of human hemoglobin autoxidation by sodium n-dodecyl sulfate. Journal of Biochemistry and Molecular Biology 35(4), 364-370. http://dx.doi.org/

Rhodes S, Farwell A, Hewitt LM, MacKinnon M, Dixon DG. 2005. The effects of dimethylated and alkylated  polycyclic  aromatic  hydrocarbons  on  the embryonic  development  of  the  Japanese  medaka. Ecotoxicology and Environmental Safety 60(3), 247-258. http://www.ncbi.nlm.nih.gov/pubmed/15590001

Rifkind JM. 1974. Copper and the autoxidation of haemoglobin. Biochemistry 13(12), 2475-2481. http://pubs.acs.org/doi/pdf/10.1021/bi00709a003

Wallace WJ, Houtchens RA, Maxwell JC, Caughey WS. 1982. Mehanism of autooxidation for haemoglobins and myoglobins: Promotion of superoxide production by protons and anions. The Journal of Biological Chemistry 257(9), 4966-4977. http://www.jbc.org/content/257/9/4966

Zavodnik IB, Piletskaia TP, Stepuro II. 1992. Auto-oxidation and oxygenation of human haemoglobin. Molecular Biology 26(2), 321-327. http://www.ncbi.nlm.nih.gov/pubmed/1339953