Catalytic pathways of Euphorbia characias peroxidase reacting with hydrogen peroxide
-
Anna Mura
Abstract
The reaction of Euphorbia characias latex peroxidase (ELP) with hydrogen peroxide as the sole substrate was studied by conventional and stopped-flow spectrophotometry. The reaction mechanism occurs via three distinct pathways. In the first (pathway I), ELP shows catalase-like activity: H2O2 oxidizes the native enzyme to compound I and subsequently acts as a reducing substrate, again converting compound I to the resting ferric enzyme. In the presence of an excess of hydrogen peroxide, compound I is still formed and further reacts in two other pathways. In pathway II, compound I initiates a series of cyclic reactions leading to the formation of compound II and compound III, and then returns to the native resting state. In pathway III, the enzyme is inactivated and compound I is converted into a bleached inactive species; this reaction proceeds faster in samples illuminated with bright white light, demonstrating that at least one of the intermediates is photosensitive. Calcium ions decrease the rate of pathway I and accelerate the rate of pathways II and III. Moreover, in the presence of calcium the inactive stable verdohemochrome P670 species accumulates. Thus, Ca2+ ions seem to be the key for all catalytic pathways of Euphorbia peroxidase.
References
Antonini, G., Bellelli, A., Brunori, M., and Falcioni, G. (1996). Kinetic and spectroscopic properties of the cyanide complex of ferrous hemoglobins I and IV from trout blood. Biochem. J.314, 533–540.10.1042/bj3140533Search in Google Scholar
Baek, H.K. and Van Wart, H.E. (1992). Elementary steps in the reaction of horseradish peroxidase with several peroxides: kinetics and thermodynamics of formation of compound 0 and compound I. J. Am. Chem. Soc.114, 718–725.10.1021/ja00028a046Search in Google Scholar
Blumberg, W.E., Peisach, J., Wittenberg, B.A., and Wittenberg, J.B. (1968). An electron paramagnetic resonance and optical study of horseradish peroxidase and its derivatives. J. Biol. Chem.243, 1854–1862.10.1016/S0021-9258(18)93520-9Search in Google Scholar
Burner, U. and Obinger, C. (1997). Transient-state and steady-state kinetics of the oxidation of aliphatic and aromatic thiols by horseradish peroxidase. FEBS Lett.411, 269–274.10.1016/S0014-5793(97)00713-8Search in Google Scholar
Cardemil, E. (1987). Kinetics of the chemical modification of enzymes. In: Chemical Modification of Enzymes. J. Eyzaguirre, ed. (Chichester, UK: Ellis Horwood), pp. 23–34.Search in Google Scholar
Hernández-Ruiz, J., Arnao, M.B., Hiner, A.N.P, García-Cánovas, F., and Acosta, M. (2001). Catalase-like activity of horseradish peroxidase: relationship to enzyme inactivation by H2O2. Biochem. J.354, 107–114.10.1042/bj3540107Search in Google Scholar
Hewson, W.D. and Hager, L.P. (1979). Peroxidases, catalases, and chloroperoxidase. In: The Porphyrins, Vol. XII (New York, USA: Academic Press), pp. 295–335.10.1016/B978-0-12-220107-3.50013-XSearch in Google Scholar
Hiner, A.N.P, Rodríguez-López, J.N., Arnao, M.B., Lloyd Raven, E., García-Cánovas, F., and Acosta, M. (2000). Kinetic study of the inactivation of ascorbate peroxidase by hydrogen peroxide. Biochem. J.348, 321–328.10.1042/bj3480321Search in Google Scholar
Hiner, A.N.P, Hernández-Ruiz, J., Williams, G.A., Arnao, M.B., García-Cánovas, F., and Acosta, M. (2001). Catalase-like oxygen production by horseradish peroxidase must predominantly be an enzyme-catalyzed reaction. Arch. Biochem. Biophys.392, 295–302.10.1006/abbi.2001.2460Search in Google Scholar PubMed
Hiner, A.N.P, Hernández-Ruiz, J., Rodríguez-López, J.N., García-Cánovas, F., Brisset, N.C., Smith, A.T., Arnao, M.B., and Acosta, M. (2002). Reaction of the class II peroxidases, lignin peroxidase and Arthromyces ramosus peroxidase, with hydrogen peroxide. J. Biol. Chem.277, 26879–26885.10.1074/jbc.M200002200Search in Google Scholar PubMed
Isaac, I.S. and Dawson, J.H. (1999). Haem iron-containing peroxidases. In: Essays in Biochemistry, Vol. 34, D.P. Ballou, ed. (London, UK: Portland Press), pp. 51–69.Search in Google Scholar
Jantschko, W., Furtmuller, P.G., Zederbauer, M., Neugschwandtner, K., Jakopitsch, C., and Obinger, C. (2005). Reaction of ferrous lactoperoxidase with hydrogen peroxide and dioxygen: an anaerobic stopped-flow study. Arch. Biochem. Biophys.434, 51–59.10.1016/j.abb.2004.10.014Search in Google Scholar PubMed
Medda, R., Padiglia, A., Longu, S., Bellelli, A., Arcovito, A., Cavallo, S., Pedersen, J.Z., and Floris, G. (2003). Critical role of Ca2+ ions in the reaction mechanism of Euphorbia characias peroxidase. Biochemistry42, 8909–8918.10.1021/bi034609zSearch in Google Scholar
Mura, A., Medda, R., Longu, S., Floris, G., Rinaldi, A.C., and Padiglia, A. (2005). A Ca2+/calmodulin-binding peroxidase from Euphorbia latex: novel aspect of calcium-hydrogen peroxide cross-talk in the regulation of plant defense. Biochemistry44, 14120–14130.10.1021/bi0513251Search in Google Scholar
Passardi, F., Cosio, C., Penel, C., and Dunand, C. (2005). Peroxidases have more functions than a Swiss army knife. Plant Cell Rep.24, 255–265.10.1007/s00299-005-0972-6Search in Google Scholar
Poulos, T.L. and Kraut, J. (1980). The stereochemistry of peroxidase catalysis. J. Biol. Chem.255, 8199–8205.10.1016/S0021-9258(19)70630-9Search in Google Scholar
Poulos, T.L., Edwards, S.L., Wariishi, H., and Gold, M.H. (1993). Crystallographic refinement of lignin peroxidase at 2 Å. J. Biol. Chem.268, 4429–4440.10.1016/S0021-9258(18)53627-9Search in Google Scholar
Rasmussen, C.B., Henriksen, A., Abelskov, K., Jensen, R.B., Rasmussen, S.K., Hejgaard, J., and Welinder, K.G. (1997). Purification, characterization and stability of barley grain peroxidase BP1, a new type of plant peroxidase. Physiol. Plant.100, 102–110.10.1111/j.1399-3054.1997.tb03459.xSearch in Google Scholar
Rodriguez-Lopez, J.N., Hernández-Ruiz, J., García-Cánovas, F., Thorneley, R.N.F., Acosta, M., and Arnao, M.B. (1997). The inactivation and catalytic pathways of horseradish peroxidase with m-chloroperoxybenzoic acid. J. Biol. Chem.272, 5469–5476.10.1074/jbc.272.9.5469Search in Google Scholar
Roman, R. and Dunford, H.B. (1972). pH dependence of the oxidation of iodide by Compound I of horseradish peroxidase. Biochemistry11, 2076–2083.10.1021/bi00761a013Search in Google Scholar
Sutherland, G.R.J., Zapanda, L.S., Tien, M., and Aust, S.D. (1997). Role of calcium in maintaining the heme environment in manganese peroxidase. Biochemistry36, 3654–3662.10.1021/bi962195mSearch in Google Scholar
Welinder, K.G. (1985). Plant peroxidases. Their primary, secondary and tertiary structures, and relation to cytochrome c peroxidase. Eur. J. Biochem.151, 497–450.Search in Google Scholar
Welinder, K.G. (1992). Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol.2, 388–393.10.1016/0959-440X(92)90230-5Search in Google Scholar
Yamada, H. and Yamazaki, I. (1974). Proton balance in conversions between five oxidation-reduction states of horseradish peroxidase. Arch. Biochem. Biophys.165, 728–738.10.1016/0003-9861(74)90301-4Search in Google Scholar
©2006 by Walter de Gruyter Berlin New York
Articles in the same Issue
- Protein aggregation in crowded environments
- Nitrite, a naturally occurring precursor of nitric oxide that acts like a ‘prodrug’
- Functional studies of the small subunit of EcoHK31I DNA methyltransferase
- Functional analysis of amino acid residues at the dimerisation interface of KpnI DNA methyltransferase
- Conformation and stability of the Streptococcus pyogenes pSM19035-encoded site-specific β recombinase, and identification of a folding intermediate
- Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of α-sarcin
- Pathogenicity of catalytic antibodies: catalytic activity of Bence Jones proteins from myeloma patients with renal impairment can elicit cytotoxic effects
- Transgenic expression of gallerimycin, a novel antifungal insect defensin from the greater wax moth Galleria mellonella, confers resistance to pathogenic fungi in tobacco
- Catalytic pathways of Euphorbia characias peroxidase reacting with hydrogen peroxide
- Biochemical and pharmacological characterization of the human bradykinin subtype 2 receptor produced in mammalian cells using the Semliki Forest virus system
- A spectroscopic analysis of the interaction between the human regulatory proteins RACK1 and Ki-1/57
- Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains
- The gating effect of calmodulin and calcium on the connexin50 hemichannel
- C-Terminal fusion of eGFP to the bradykinin B2 receptor strongly affects down-regulation but not receptor internalization or signaling
- Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII
- μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation
- Cathepsin L splice variants in human breast cell lines
Articles in the same Issue
- Protein aggregation in crowded environments
- Nitrite, a naturally occurring precursor of nitric oxide that acts like a ‘prodrug’
- Functional studies of the small subunit of EcoHK31I DNA methyltransferase
- Functional analysis of amino acid residues at the dimerisation interface of KpnI DNA methyltransferase
- Conformation and stability of the Streptococcus pyogenes pSM19035-encoded site-specific β recombinase, and identification of a folding intermediate
- Tyr-48, a conserved residue in ribotoxins, is involved in the RNA-degrading activity of α-sarcin
- Pathogenicity of catalytic antibodies: catalytic activity of Bence Jones proteins from myeloma patients with renal impairment can elicit cytotoxic effects
- Transgenic expression of gallerimycin, a novel antifungal insect defensin from the greater wax moth Galleria mellonella, confers resistance to pathogenic fungi in tobacco
- Catalytic pathways of Euphorbia characias peroxidase reacting with hydrogen peroxide
- Biochemical and pharmacological characterization of the human bradykinin subtype 2 receptor produced in mammalian cells using the Semliki Forest virus system
- A spectroscopic analysis of the interaction between the human regulatory proteins RACK1 and Ki-1/57
- Subcellular localisation of human inositol 1,4,5-trisphosphate 3-kinase C: species-specific use of alternative export sites for nucleo-cytoplasmic shuttling indicates divergent roles of the catalytic and N-terminal domains
- The gating effect of calmodulin and calcium on the connexin50 hemichannel
- C-Terminal fusion of eGFP to the bradykinin B2 receptor strongly affects down-regulation but not receptor internalization or signaling
- Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII
- μ-Calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation
- Cathepsin L splice variants in human breast cell lines
