Heterogeneous inhibition of horseradish peroxidase activity by cadmium

Biochimica et Biophysica Acta - General Subjects

Volumn 1621, Issue 2, 2003, Pages 140-148

  Keyhani, Jacqueline ^a   Keyhani, Ezzatollah ^a,b   Einollahi, Nahid ^c   Minai Tehrani, Dariush ^b   Zarchipour, Sekineh ^b  

^a Laboratory for Life Sciences   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

^c TEHRAN UNIVERSITY OF MEDICAL SCIENCES   (Iran)

Author keywords

Cadmium; Cooperativity; Enzyme inhibition; Horseradish peroxidase; O dianisidine

Indexed keywords

CADMIUM; DIANISIDINE; HORSERADISH PEROXIDASE; HYDROGEN PEROXIDE;

ABSORPTION; ARTICLE; BINDING AFFINITY; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME INHIBITION; INCUBATION TIME; OXIDATION; PRIORITY JOURNAL; SPECTROPHOTOMETRY; STEADY STATE;

ARMORACIA RUSTICANA;

EID: 0037414510     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-4165(03)00053-9     Document Type: Article

References (34)

1. Cadmium and cadmium compounds. IARC Monographs on the Evaluation of Carcinogenic Risks to Human, vol. 58, Beryllium, Cadmium, Mercury and Exposure in the Glass Manufacturing Industry. 1993;119-237 IARC, Lyon.
2. Lin C.-J., Wu K.-H., Yew F.-H., Lee T.-C. Differential cytotoxicity of cadmium to rat embryonic fibroblasts and human skin fibroblasts. Toxicol. Appl. Pharmacol. 133:1995;20-26.
3. Baldrian P., in Der Wiesche C., Gabriel J., Nerud F., Zadrazil F. Influence of cadmium and mercury on activities of ligninolytic enzymes and degradation of polycyclic aromatic hydrocrabons by Pleurotus ostreatus in soil. Appl. Environ. Microbiol. 66:2000;2471-2478.
4. 2+ stores in intestinal epithelium. Biochim. Biophys. Acta. 902:1987;247-252.
5. Ogoshi K., Nanzai Y., Moriyama T. Decrease in bone strength of cadmium-treated young and old rats. Arch. Toxicol. 66:1992;315-320.
6. 2+. J. Bacteriol. 133:1978;75-80.
7. Müller T., Schuckelt R., Jaenicke L. Cadmium/zinc-metallothionein induces DNA strand breaks in vitro. Arch. Toxicol. 65:1991;20-26.
8. Coogan T.P., Bare P.M., Waalkes M.P. Cadmium-induced DNA strand damage in cultured liver cells: reduction in cadmium genotoxicity following zinc pretreatment. Toxicol. Appl. Pharmacol. 113:1992;227-233.
9. Ouariti O., Gouia H., Ghorbal M.H. Responses of bean and tomato plants to cadmium: growth, mineral nutrition and nitrate reduction. Plant Physiol. Biochem. 35:1997;347-354.
10. Yamazaki I. Peroxidase. Hayaishi O. Molecular Mechanisms of Oxygen Activation. 1974;535-558 Academic Press, New York.
11. Pruitt K.M., Kamau D.N., Miller K., Mansson-Rahemtulla B., Rahemtulla F. Quantitative, standardized assays for determining the concentrations of bovine lactoperoxidase, human salivary peroxidase, and human myeloperoxidase. Anal. Biochem. 19:1990;1278-1286.
12. Robinson D.S. Peroxidases and their significance in fruits and vegetables. Fox P.F. Food Enzymology. vol. 1:1991;399-425 Elsevier, Amsterdam.
13. Wada H., Koshiba T., Matsui T., Satô M. Involvement of peroxidase in differential sensitivity to γ-radiation in seedlings of two Nicotiana species. Plant Sci. 132:1998;109-119.
14. Mehlhorn H. Ethylene-promoted ascorbate peroxidase activity protects plants against hydrogen peroxide, ozone and paraquat. Plant Cell Environ. 13:1990;971-976.
15. Welinder K.G. Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidases. Eur. J. Biochem. 151:1985;497-504.
16. Melo N.S., Larsen E., Welinder K.G., Fevereiro P.S. Characterization of two major cationic peroxidases from cell suspension cultures of Vaccinium myrtillus. Plant Sci. 122:1997;1-10.
17. Christensen J.H., Bauw G., Welinder K.G., Van Montagu M., Boerjan W. Purification and characterization of peroxidases correlated with lignification in Poplar Xylem. Plant Physiol. 118:1998;125-135.
18. Richards K.D., Schott E.J., Sharma Y.K., Davis K.R., Gardner R.C. Aluminum induces oxidative stress genes in Arabidopsis thaliana. Plant Physiol. 116:1998;409-418.
19. Fieldes M.A., Gerhardt K.E. Flax guaiacol peroxidases can be used to illustrate the possibility of misinterpreting the effects of stress on the activity of developmentally regulated enzymes. Plant Sci. 132:1998;89-99.
20. 2 detoxifying enzymes in green and greening barley seedlings under cadmium stress. Plant Sci. 160:2001;1085-1093.
21. Converso D.A., Fernandez M.E., Tomaro M.L. Cadmium inhibition of a structural wheat peroxidase. J. Enzyme Inhib. 15:2000;171-183.
22. ++. Eur. Biophys. J. 29:2000;285.
23. Youngs H.L., Sundaramoorthy M., Gold M.H. Effects of cadmium on manganese peroxidase competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur. J. Biochem. 267:2000;1761-1769.
24. Worthington C.C. Worthington Enzyme Manual: Enzymes and Related Biochemicals. 1988;254-260 Freehold, New Jersey.
25. Chance B., Maehly A.C. Assay of catalases and peroxidases. Colowick S.P., Kaplan N.O. Methods in Enzymology. vol. II:1955;764-775 Academic Press, New York.
26. Keyhani E., Zarei M.A., Lashgarblooki-Livani T. Kinetics of peroxidases in guinea pig bone marrow under immunostimulation. FEBS Lett. 452:1999;233-236.
27. Abelskov A.K., Smith A.T., Rasmussen C.B., Dunford H.B., Welinder K.G. pH dependence and structural interpretation of the reaction of Coprinus cinereus peroxidase with hydrogen peroxide, ferulic acid and 2,2′-azinobis(3-ethylbenzthiazoline-6-sulfonic acid). Biochemistry. 36:1997;9453-9463.
28. Casella L., Gullotti M., Poli S., Bonfa M., Ferrari R.P., Marchesini A. Spectroscopic and binding studies on the stereoselective interaction of tyrosine with horseradish peroxidase and lactoperoxidase. Biochem. J. 279:1991;245-250.
29. Schejter A., Lanir A., Epstein N. Binding of hydrogen donors to horseradish peroxidase: a spectroscopic study. Arch. Biochem. Biophys. 174:1976;36-44.
30. Morishima I., Kurono M., Shiro Y. Presence of endogenous calcium ion in horseradish peroxidase. Elucidation of metal-binding site by substitutions of divalent and lanthanide ions for calcium and use of metal-induced NMR (1H and 113Cd) resonances. J. Biol. Chem. 261:1986;9391-9399.
31. Gajhede M., Schuller D.J., Henriksen A., Smith A.T., Poulos T.L. Crystal structure of horseradish peroxidase C at 2.15 Å resolution. Nat. Struct. Biol. 4:1997;1032-1038.
32. Tanaka M., Ishimori K., Morishima I. Structural roles of the highly conserved glu residue in the heme distal site of peroxidases. Biochemistry. 37:1998;2629-2638.
33. Chattopadhyay K., Mazumdar S. Structural and conformational stability of horseradish peroxidase: effect of temperature and pH. Biochemistry. 39:2000;263-270.
34. Rodríguez Marañón M.J., Stillman M.J., van Huystee R.B. Co-dependency of calcium and porphyrin for an integrated molecular structure of peanut peroxidase: a circular dichroism analysis. Biochem. Biophys. Res. Commun. 194:1993;326-332.