Skip to main content
PMC home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1990 Jan;87(1):389–393. doi: 10.1073/pnas.87.1.389

Manganese(II) catalyzes the bicarbonate-dependent oxidation of amino acids by hydrogen peroxide and the amino acid-facilitated dismutation of hydrogen peroxide.

B S Berlett 1, P B Chock 1, M B Yim 1, E R Stadtman 1
PMCID: PMC53269  PMID: 2296594

Abstract

In bicarbonate/CO2 buffer, Mn(II) and Fe(II) catalyze the oxidation of amino acids by H2O2 and the dismutation of H2O2. As the Mn(II)/Fe(II) ratio is increased, the yield of carbonyl compounds per mole of leucine oxidized is essentially constant, but the ratio of alpha-ketoisocaproate to isovaleraldehyde formed increases, and the fraction of H2O2 converted to O2 increases. In the absence of Fe(II), the rate of Mn(II)-catalyzed leucine oxidation is directly proportional to the H2O2, Mn(II), and amino acid concentrations and is proportional to the square of the HCO3- concentration. The rate of Mn(II)-catalyzed O2 production in the presence of 50 mM alanine or leucine is about 4-fold the rate observed in the absence of amino acids and accounts for about half of the H2O2 consumed; the other half of the H2O2 is consumed in the oxidation of the amino acids. In contrast, O2 production is increased nearly 18-fold by the presence of alpha-methylalanine and accounts for about 90% of the H2O2 consumed. The data are consistent with the view that H2O2 decomposition is an inner sphere (cage-like) process catalyzed by a Mn coordination complex of the composition Mn(II), amino acid, (HCO3-)2. Oxidation of the amino acid in this complex most likely proceeds by a free radical mechanism involving hydrogen abstraction from the alpha-carbon as a critical step. The results demonstrate that at physiological concentrations of HCO3- and CO2, Mn(II) is able to facilitate Fenton-type reactions.

Full text

PDF
393

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Archibald F. S., Fridovich I. The scavenging of superoxide radical by manganous complexes: in vitro. Arch Biochem Biophys. 1982 Apr 1;214(2):452–463. doi: 10.1016/0003-9861(82)90049-2. [DOI] [PubMed] [Google Scholar]
  2. Beyer W. F., Jr, Fridovich I. Characterization of a superoxide dismutase mimic prepared from desferrioxamine and MnO2. Arch Biochem Biophys. 1989 May 15;271(1):149–156. doi: 10.1016/0003-9861(89)90265-8. [DOI] [PubMed] [Google Scholar]
  3. Cheton P. L., Archibald F. S. Manganese complexes and the generation and scavenging of hydroxyl free radicals. Free Radic Biol Med. 1988;5(5-6):325–333. doi: 10.1016/0891-5849(88)90104-9. [DOI] [PubMed] [Google Scholar]
  4. Church F. C., Porter D. H., Catignani G. L., Swaisgood H. E. An o-phthalaldehyde spectrophotometric assay for proteinases. Anal Biochem. 1985 May 1;146(2):343–348. doi: 10.1016/0003-2697(85)90549-4. [DOI] [PubMed] [Google Scholar]
  5. Darr D., Zarilla K. A., Fridovich I. A mimic of superoxide dismutase activity based upon desferrioxamine B and manganese(IV). Arch Biochem Biophys. 1987 Nov 1;258(2):351–355. doi: 10.1016/0003-9861(87)90354-7. [DOI] [PubMed] [Google Scholar]
  6. Fucci L., Oliver C. N., Coon M. J., Stadtman E. R. Inactivation of key metabolic enzymes by mixed-function oxidation reactions: possible implication in protein turnover and ageing. Proc Natl Acad Sci U S A. 1983 Mar;80(6):1521–1525. doi: 10.1073/pnas.80.6.1521. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. HARDMAN J. K., STADTMAN T. C. Metabolism of amega-amino acids. III. Mechanism of conversion of gamma-aminobutyrate to gamma-hydroxybutryate by Clostridium aminobutyricum. J Biol Chem. 1963 Jun;238:2081–2087. [PubMed] [Google Scholar]
  8. Keele B. B., Jr, McCord J. M., Fridovich I. Superoxide dismutase from escherichia coli B. A new manganese-containing enzyme. J Biol Chem. 1970 Nov 25;245(22):6176–6181. [PubMed] [Google Scholar]
  9. Kono Y., Takahashi M. A., Asada K. Oxidation of manganous pyrophosphate by superoxide radicals and illuminated spinach chloroplasts. Arch Biochem Biophys. 1976 Jun;174(2):454–462. doi: 10.1016/0003-9861(76)90373-8. [DOI] [PubMed] [Google Scholar]
  10. Koppenol W. H., Levine F., Hatmaker T. L., Epp J., Rush J. D. Catalysis of superoxide dismutation by manganese aminopolycarboxylate complexes. Arch Biochem Biophys. 1986 Dec;251(2):594–599. doi: 10.1016/0003-9861(86)90368-1. [DOI] [PubMed] [Google Scholar]
  11. Levine R. L., Oliver C. N., Fulks R. M., Stadtman E. R. Turnover of bacterial glutamine synthetase: oxidative inactivation precedes proteolysis. Proc Natl Acad Sci U S A. 1981 Apr;78(4):2120–2124. doi: 10.1073/pnas.78.4.2120. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Levine R. L. Oxidative modification of glutamine synthetase. I. Inactivation is due to loss of one histidine residue. J Biol Chem. 1983 Oct 10;258(19):11823–11827. [PubMed] [Google Scholar]
  13. Stadtman E. R., Berlett B. S., Chock P. B. Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer. Proc Natl Acad Sci U S A. 1990 Jan;87(1):384–388. doi: 10.1073/pnas.87.1.384. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Stadtman E. R., Wittenberger M. E. Inactivation of Escherichia coli glutamine synthetase by xanthine oxidase, nicotinate hydroxylase, horseradish peroxidase, or glucose oxidase: effects of ferredoxin, putidaredoxin, and menadione. Arch Biochem Biophys. 1985 Jun;239(2):379–387. doi: 10.1016/0003-9861(85)90703-9. [DOI] [PubMed] [Google Scholar]
  15. Thurman R. G., Ley H. G., Scholz R. Hepatic microsomal ethanol oxidation. Hydrogen peroxide formation and the role of catalase. Eur J Biochem. 1972 Feb;25(3):420–430. doi: 10.1111/j.1432-1033.1972.tb01711.x. [DOI] [PubMed] [Google Scholar]
  16. Weisiger R. A., Fridovich I. Superoxide dismutase. Organelle specificity. J Biol Chem. 1973 May 25;248(10):3582–3592. [PubMed] [Google Scholar]
  17. Yim M. B., Berlett B. S., Chock P. B., Stadtman E. R. Manganese(II)-bicarbonate-mediated catalytic activity for hydrogen peroxide dismutation and amino acid oxidation: detection of free radical intermediates. Proc Natl Acad Sci U S A. 1990 Jan;87(1):394–398. doi: 10.1073/pnas.87.1.394. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES