Abstract
Bicarbonate anion (HCO -3 ) is present at high concentration (25 mM) in biological fluids. At this HCO3 concentration, the carbon-di-oxide (CO2) concentration is estimated to be ca. 1.2 mM at physiological conditions. A major function of the HCO -3 CO2 couple in biological systems is to regulate pH. Although HCO -3 -mediated enhancement of luminol oxidation was reported several decades ago (Hodgson and Fridovich, 1976), only recently was the role of HCO -3 recognized in biological oxidations (Denicola et al 1996; Ischiropoulos et al 1992; Lymar et al 1996; Singh et al 1998; Zhang et al 1997).
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References
Beckman, J. S., 1996, Oxidative damage and tyrosine nitration by peroxynitrite Chem. Res. Toxicol. 9: 836–844.
Beckman, J. S., Beckman, T. W., Chen, J., Marshall, P. A., and Freeman, B.A., 1990, Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide Proc. Natl. Acad. Sci. USA 87: 1620–1624.
Bonini, M. G., Radi, R., Ferrer-Sueta, G., Ferreira, A. M. D. C., and Augusto, O., 1999, Direct EPR detection of the carbonate radical anion produced from peroxynitrite and carbon dioxide J Biol. Chem. 274: 10802–10806.
Denicola, A., Freeman, B. A., Trujillo, M., and Radi, R., 1996, Peroxynitrite reaction with carbon dioxide/bicarbonate: kinetics and influence on peroxynitrite-mediated oxidations Arch. Biochem. Biophys. 333: 49–58.
Eiserich, J. P., Hristova, M., Cross, C. E., Jones, A. D., Freeman, B. A., Halliwell, B., and Van der Vliet, A., 1998, Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase and neutrophils Nature 391: 393–397.
Goss, S. P. A., Singh, R. J., and Kalyanaraman, B., 1999, Bicarbonate enhances the peroxidase activity of Cu,Zn-superoxide dismutase—role of carbonate anion radical J. Biol. Chem. 274: 28233–28239.
Hodgson, E. K., and Fridovich, I., 1975a, The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: inactivation of the enzyme Biochemistry 14: 5294–5298.
Hodgson, E. K., and Fridovich, I., 1975b, The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide: chemiluminescence and peroxidation Biochemistry 14: 5299–5303.
Hodgson, E. K., and Fridovich, I., 1976, The mechanism of the activity-dependent luminescence of xanthine oxidase Arch. Biochem. Biophys. 172: 202–205.
Ischiropoulos, H., 1998, Biological tyrosine nitration: a pathophysiological function of nitric oxide and reactive nitrogen species Arch. Biochem. Biophys. 356: 1–11.
Ischiropoulos, H., Zu, Li., Chen, J., Tsai, M., Martin, J. C., Smith, C. D., and Beckman, J. S., 1992, Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase Arch. Biochem. Biophys. 298: 438–445.
Jacob, J. S., Cistola, D. P., Hsu, F. F., Muzaffar, S., Mueller, D. M., Hazen, S. L., and Heinecke, J. W., 1996, Human phagocytes employ the myeloperoxidase-hydrogen peroxide system to synthesize dityrosine, trityrosine, pulcherosine, and isodityrosine by a tyrosyl radical-dependent pathway J. Biol. Chem. 271: 19950–19956.
Liochev, S. I., and Fridovich, I., 1999, On the role of bicarbonate in peroxidations catalyzed by Cu,Zn superoxide dismutase Free Radic. Biol. Med. 27: 1444–1447.
Lymar, S. B., Jiang, Q., and Hurst, J. K., 1996, Mechanism of carbon dioxide-catalyzed oxidation of tyrosine by peroxynitrite Biochemistry 35: 7855–7881.
Sankarapandi, S., and Zweier, J., 1999, Bicarbonate is required for the peroxidase activity of Cu,Zn-superoxide dismutase at physiological pH J. Biol. Chem. 274: 1226–1232.
Singh, R. J., Goss, S. P. A., Joseph, J., and Kalyanaraman, B,1998, Nitration of γ-tocopherol and oxidation of a-tocopherol by Cu,ZnSOD/H2O2/N0: role of nitrogen dioxide free radical Proc. Natl. Acad. Sci. USA 95: 12912–12917.
Singh, R. J., Karoui, H., Gunther, M. R., Beckman, J. S., Mason, R. P., and Kalyanaraman, B., 1998, Reexamination of the mechanism of hydroxyl radical adducts formed from the reaction between familial amyotrophic lateral sclerosis-associated Cu,Zn superoxide dismutase mutants and H2O2 Proc. Natl. Acad. Sci. USA 95: 6675–6680.
Wiedau-Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., and Bredesen, D. E., 1996, Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis Science 271: 515–518.
Yim, M. B., Chock, P. B,and Stadtman, E. R., 1993, Enzyme function of copper,zinc superoxide dismutase as a free radical generator J. Biol. Chem. 274: 1226–1232.
Yim, M. B., Kang, J.-H., Yim, H.-S., Kwak, H.-S., Chock, P. B,and Stadtman, E. R., 1996, A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Znsuperoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Kmfor hydrogen peroxide Proc. Natl. Acad. Sci. USA 93:5709–5714.
Zhang, H., Squadrito, G. C., and Pryor, W. A., 1997, The mechanism of the peroxynitritecarbon dioxide reaction proved using tyrosine Nitric Oxide: Biology and Chemistry 1:301–307.
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Kalyanaraman, B., Joseph, J., Zhang, H. (2001). Bicarbonate Enhances Nitration and Oxidation Reactions in Biological Systems—Role of Reactive Oxygen and Nitrogen Species. In: Dansette, P.M., et al. Biological Reactive Intermediates VI. Advances in Experimental Medicine and Biology, vol 500. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0667-6_23
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