PL EN


Preferences help
enabled [disable] Abstract
Number of results
2009 | 56 | 3 | 509-513
Article title

Flavonoids as reductants of ferryl hemoglobin

Content
Title variants
Languages of publication
EN
Abstracts
EN
The ferryl derivatives of hemoglobin are products of the reactions of oxy- and methemoglobin with hydrogen peroxide. Ferryl hemoglobins, either with or without a radical site on the protein moiety, are oxidizing species. Plant polyphenols, flavonoids, have been shown to act as antioxidants in vivo and in vitro. Reactions of met- and oxyhemoglobin with hydrogen peroxide in the presence of catechin, quercetin and rutin were studied. These flavonoids accelerated reduction of ferryl hemoglobin to methemoglobin. The rate constants of the reactions of ferryl hemoglobin with catechin, quercetin and rutin were in the order of 102 M-1 s-1, i.e. similar to the rate constants of ferryl hemoglobin with intracellular reducing compounds like urate or ascorbate. The beneficial effect of flavonoids against oxidative damage of hemoglobin caused by hydroperoxides, reported in the literature, is probably, at least in part, connected with the ability of flavonoids to scavenge ferryl hemoglobin.
Year
Volume
56
Issue
3
Pages
509-513
Physical description
Dates
published
2009
received
2009-06-15
revised
2009-08-21
accepted
2009-09-16
(unknown)
2009-09-17
References
  • Antonini E, Brunori M (1971) Hemoglobin and Myoglobin in their Reactions with Ligands. North Holland, Amsterdam.
  • Carrel RW, Winterbourn CC, Rachmilevitz EA (1975) Activated oxygen and haemolysis. Br J Haematol 30: 259-264.
  • Cesquini M, Torsoni MA, Stoppa GR, Ogo SH (2003) t-BOOH-induced oxidative damage in sicle red blood cells and the role of flavonoids. Biomed Pharmacother 57: 124-129.
  • Cooper CE, Silaghi-Dumitrescu R, Rukengwa M, Alayash AI, Buehler PW (2008) Peroxidase activity of hemoglobin towards ascorbate and urate: A synergistic protective strategy against toxicity of Hemoglobin-Based Oxygen Carriers (HBOC). Biochim Biophys Acta 1784: 1415-1420.
  • Cotelle N (2001) Role of flavonoids in oxidative stress. Curr Top Med Chem 1: 569-590.
  • Everse J, Johnson MC, Marini MA (1994) Peroxidative activities of hemoglobin and hemoglobin derivatives. Methods Enzymol 231: 547-561.
  • Everse J, Hsia N (1997) The toxicities of native and modified hemoglobins. Free Radic Biol Med 22: 1075-1099.
  • Giulivi C, Davies KJA (1990) A novel antioxidant role for haemoglobin. The comproportionation of ferrylhemoglobin with oxyhemoglobin. J Biol Chem 265: 19453-19460.
  • Giulivi C, Davies KJA (1994) Hydrogen peroxide-mediated ferrylhemoglobin generation in vitro and in red blood cells. Methods Enzymol 231: 490-496.
  • Goldman DW, Breyer III RJ, Yeh D, Brockner-Ryan A, Alayash AI (1998) A cellular haemoglobin-mediated oxidative stress toward endothelium: a role of ferryl iron. Am J Physiol Heart Circ Physiol 275: H1046-H1053.
  • Grinberg LN, Rachmilewitz EA, Newmark H (1994) Protective effects of rutin against haemoglobin oxidation. Biochem Pharmacol 48: 643-649.
  • Heim KE, Tagliaferro AR, Bobilya DJ (2002) Flavonoid antioxidants: chemistry, metabolism and structure-activity relationships. J Nutr Biochem 13: 572-584.
  • Herold S, Rehmann F-J (2003) Kinetics of the reactions of nitrogen monoxide and nitrite with ferryl haemoglobin. Free Radic Biol Med 34: 531-545.
  • Jia Y, Alayash AI (2008) Effects of (-)epigallicatechin gallate on the redox reactions of human hemoglobin. Free Radic Biol Med 45: 659-666.
  • Kanner J, Harel S (1985) Initiation of membrane lipid peroxidation by activated metmyoglobin and methemoglobin. Arch Biochem Biophys 237: 314-321.
  • Kowalczyk A, Puchala M, Wesolowska K, Serafin E (2007) Inactivation of alcohol dehydrogenase (ADH) by ferryl derivatives of human hemoglobin. Biochim Biophys Acta 1774: 86-92.
  • McArthur KM, Davies MJ (1993) Detection and reactions of the globin radical in hemoglobin. Biochim Biophys Acta 1202: 173-181.
  • Misra HP, Fridovich I (1972) The generation of superoxide anion during the autooxidation of haemoglobin. J Biol Chem 247: 6960-6962.
  • Mochizuki M, Yamazaki S, Kano K, Ikeda T (2002) Kinetic analysis and mechanistic aspects of autooxidation of catechins. Biochim Biophys Acta 1569: 35-44.
  • Munoz-Munoz JL, Garcia-Molina F, Molina-Alarcon M, Tudela J, Garcia-Canovas F, Rodriguez-Lopez JN (2008) Kinetic characterization of the enzymatic and chemical modification of the catechins in green tea. J Agric Food Chem 56: 9215-9224.
  • Nagababu E, Rifkind JM (2000) Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry 39: 12503-12511.
  • Nagababu E, Ramasamy S, Rifkind JM, Jia Y, Alayash AI (2002) Site-specific cross linking of human and bovine hemoglobins differentially alters oxygen binding and redox reactions producing rhombic heme and heme degradation. Biochemistry 41: 7407-7415.
  • Patel RP, Svistunenko DA, Darley-Usmar V, Symons MCR, Wilson MT (1996) Redox cycling of human methaemoglobin by H2O2 yields persistent ferryl iron and protein-based radicals. Free Radic Res 25: 117-123.
  • Pereira AL, Cesquini M, Tomizawa E, Torsoni MA, Ogo SH (2003) The beneficial effect of three flavonols against oxidative damage. J Food Biochem 27: 141-152.
  • Sztiller M, Puchala M, Kowalczyk A, Bartosz G (2006) The influence of ferrylhemoglobin and methemoglobin on the human erythrocyte membrane. Redox Rep 11: 263-271.
  • Tesoriere L, Allegra M, D'Arpa D, Butera D, Livrea MA (2001) Reaction of melatonin with hemoglobin-derived oxoferryl radicals and inhibition of the hydroperoxide-induced hemoglobin denaturation in red blood cells. J Pineal Res 31: 114-119.
  • Winterbourn CC (1990) Oxidative reactions of hemoglobin. Methods Enzymol 186: 265-272.
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv56p509kz
Identifiers
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.