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Journal of Biological Sciences

Year: 2005 | Volume: 5 | Issue: 1 | Page No.: 44-49
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Research Article

Microperoxidase 8 as a Powerful Tool for Biological Applications

Remy Ricoux, Hafsa Korri-Youssoufi and Jean-Pierre Mahy

ABSTRACT

Microperoxidase 8 is a heme octapeptide obtained by hydrolytic digestion of cytochrome which contains the heme prosthetic group together with the amino acid residues 14 to 21 of horse cytochrome c, including His 18, whose imidazole group acts as the fifth axial ligand of the iron. It is a very good model for the coordination properties and the reactivity of hemoproteins like peroxidases and cytochromes P450. Indeed, it is first able to bind a wide variety of ligands on the 6th axial coordination position of the iron. Second, it is able to perform peroxidase-like reactions, such as the nitration of phenol by H2O2/NO2-, the oxidation of N-hydroxyguanidines with formation of nitrogen oxides. Third, it is also able to catalyze monooxygenase-like reactions, such as the N-dealkylation of aromatic amines and the O-dealkylation of aromatic ethers, the para-hydroxylation of aniline, the monooxygenation of polycyclic aromatic compounds and the S-oxidation of sulfides. In the later case no selectivity was observed with MP8 alone, whereas when MP8 was associated with a monoclonal antibody raised against it, the oxidation was stereoselective with a 45% enantiomeric excess in favor of the R isomer. This association constituted a new generation of artificial hemoproteins based on a monoclonal antibody, which we named "hemoabzyme" and which appeared as a promising biocatalyst for selective oxidation reactions. Finally, a new biomedical application has recently been found for MP8 as a biosensor for molecules of biological interest. For this, several strategies were envisioned to immobilize MP8 at the surface of an electrode, in such a way that the 6th coordination position of the iron may be accessible to ligands. Detection of the target molecule will then be realized upon measurement of the variations of the redox potential and of the current intensity induced by its binding on the iron of MP8.
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REFERENCES

  1. Mansuy, D., P. Battioni and J.P. Battioni, 1989. Chemical model systems for drug-metabolizing cytochrome-P-450-dependent monooxygenases. Eur. J. Biochem., 184: 267-285.
  2. Aron, J., D.A. Baldwin, H.M. Marques, J.M. Pratt and P.A. Adams, 1986. Hemes and hemoproteins 1: Preparation and analysis of heme containing octapeptide (Microperoxidase-8) and identification of the monomeric form in aqueous solution. J. Inorg. Biochem., 27: 227-243.
    Direct Link
  3. Munro, O.Q. and H.M. Marques, 1996. Heme-peptide models for hemoproteins. 1. Solution chemistry of N-Acetylmicroperoxidase-8. Inorg. Chem., 35: 3752-3767.
  4. Othman, S., A. Le-Lirzin and A. Desbois, 1994. A resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: Characterization of the bis (histidine) axial ligation in c-type cytochromes. Biochemistry, 33: 15437-15448.
  5. Carraway, A.D., S.L. Povlock, M.L. Houston, D.S. Johnston and J. Peterson, 1995. Monomeric ferric heme peptide derivatives: Model systems for hemoproteins. J. Inorg. Biochem., 60: 267-276.
  6. Marques, H.M., D.A. Baldwin and J.M. Pratt, 1987. Hemes and hemoproteins. 3. The reaction of microperoxidase-8 with cyanide: Comparison with aquocobalamin and hemoproteins. J. Inorg. Biochem., 29: 77-91.
  7. Baldwin, D.A., H.M. Marques,and J.M. Pratt, 1986. Hemes and hemeproteins, 2: The pH-dependent equilibria of microperoxidase-8 and characterization of the coordination sphere of Fe (III). J. Inorg. Biochem., 27: 245-254.
    PubMed
  8. Hamza, M.S.A. and J.M. Pratt, 1994. Hemes and hemoproteins. Part 10. Co-ordination of imidazole and other azoles by the iron (III) porphyrin microperoxidase-8. J. Chem. Soc., Dalton Trans., 9: 1367-1371.
  9. Marques, H.M., M.P. Byfield and J.M. Pratt, 1993. Hemes and hemoproteins. Part 7. Co-ordination of ammonia, aniline and pyridine by the iron (III) porphyrin microperoxidase-8. J. Chem. Soc. Dalton Trans., 11: 1633-1639.
  10. Marques, H.M. and A. Rousseau, 1996. Reactions of ferric porphyrins and thiols. The reaction of the haem octapeptide, N-acetylmicroperoxidase-8, with cysteine. Inorg. Chim. Acta, 248: 115-119.
  11. Lefevre-Groboillot, D., S. Dijols, J.L. Boucher, J.P. Mahy and R. Ricoux et al., 2001. N-hydroxyguanidines as new heme ligands: UV-visible, EPR and resonance Raman studies of the interaction of various compounds bearing a C=NOH function with microperoxidase-8. Biochemistry, 40: 9909-10017.
  12. Blumenthal, D.C. and R.J. Kassner, 1980. For anion binding to the active site of high spin ferric heme proteins. J. Biol. Chem., 255: 5859-5863.
  13. Baumgartner, C.P., M. Sellers, R. Nassif and L. May, 1974. Mossbauer studies of some complexes of the undecapeptide of cytochrome c. Eur. J. Biochem., 46: 625-629.
  14. Marques, H.M., I. Cukrowski and P.R. Vashi, 2000. Co-ordination of weak field ligands by N-acetylmicroperoxidase-8 (NAcMP8), a ferric haempeptide from cytochrome c and the influence of the axial ligand on the reduction potential of complexes of NAcMP8. J. Chem. Soc. Dalton Trans., 8: 1335-1342.
  15. Marques, H.M., K. Voster and T.J. Egan, 1996. The interaction of the heme-octapeptide, N-acetylmicroperoxidase-8 with antimalarial drugs: Solution studies and modeling by molecular mechanics methods. J. Inorg. Biochem., 64: 7-23.
  16. Sharma, V.S., R.A. Isaacson, M.E. John, M.R. Waterman and M. Chevion, 1983. Reaction of nitric oxide with heme proteins: Studies on metmyoglobin, opossum methemoglobin and microperoxidase. Biochemistry, 22: 3897-3902.
  17. Sharma, V.S., M.R. Schmidt and H.M. Ranney, 1976. Dissociation of CO from carboxyhemoglobin. J. Biol. Chem., 251: 4267-4272.
  18. Othman, S., A. Le-Lirzin and A. Desbois, 1994. A resonance Raman investigation of imidazole and imidazolate complexes of microperoxidase: Characterization of the bis(histidine) axial ligation in c-type cytochromes. Biochemistry, 33: 15437-15448.
  19. Othman, S. and A. Desbois, 1998. Resonance Raman investigation of lysine and N-acetylmethionine complexes of ferric and ferrous microperoxidase. Eur. Biophys. J., 28: 12-25.
  20. Ricoux, R., J.L. Boucher, D. Mansuy and J.P. Mahy, 2000. Formation of iron(II)-nitrosoalkane complexes: A new activity of microperoxidase 8. Biochem. Biophys. Res. Commun., 278: 217-223.
  21. Baldwin, D.A., H. Marques and J.M. Pratt, 1987. Hemes and hemoproteins 5: Kinetics of the peroxidasic activity of microperoxidase 8, model for the peroxidase enzymes. J. Inorg. Biochem., 30: 203-217.
  22. Adams, P.A., 1990. The peroxidasic activity of the heme octapeptide microperoxidase 8 (MP8), the kinetic mechanism of the catalytic reduction of H2O2 by MP8 using 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS) as a reducing substrate. J. Chem. Soc. Perkin Trans., 2: 1407-1414.
  23. Cunningham, I.D., J.L. Bachelor and J.M. Pratt, 1991. Kinetic study of the H2O2 oxidation of phenols, naphtols and anilines catalysed by the haem octapeptide microperoxidase 8. J. Chem. Soc. Perkin Trans., 2: 1839-1843.
  24. Ricoux, R., J.L. Boucher, D. Mansuy and J.P. Mahy, 2001. Microperoxidase 8 catalyzed nitration of phenol by nitrogen dioxide radicals. Eur. J. Biochem., 268: 3783-3788.
  25. Ricoux, R., J.L. Boucher, D. Mandon, Y.M. Frapart, Y. Henry, D. Mansuy and J.P. Mahy, 2003. Microperoxidase 8 catalysed nitrogen oxides formation from oxidation of N-hydroxyguanidines by hydrogen peroxide. Eur. J. Biochem., 270: 47-55.
  26. Rusvai, E., M. Vegh, M. Kramer and I. Horvat, 1988. Hydroxylation of aniline mediated by heme-bound oxy-radicals in a heme peptide model system. Biochem. Pharmacol., 37: 4574-4577.
  27. Colonna, S., N. Gagerro, G. Carrea and P. Pasta, 1994. The microperoxidase-11 catalysed oxidation of sulfides is enantioselective. Tetrahedron Lett., 35: 9103-9104.
  28. Osman, A.M., J. Koerts, M.G. Boersma, S. Boeren, C. Veeger and I. Rietjens, 1996. Microperoxidase/ H2O2-catalysed aromatic hydroxylation proceeds by a cytochrome-P450 type oxygen transfer reaction mechanism. Eur. J. Biochem., 240: 232-233.
  29. Boersma, M.G., J.L. Primus, J. Koerts, C. Veeger and I. Rietjens, 2000. Heme-(hydro) peroxide mediated O- and N-dealkylation. A study with microperoxidase. Eur. J. Biochem., 267: 6673-6678.
  30. Cochran, A.G. and P.G. Schultz, 1990. Peroxidase activity of an antibody Bheme complex. J. Am. Chem. Soc., 112: 9414-9415.
  31. Feng, Y., Z. Liu, G. Gao, S.J. Gao, X.Y. Liu and T.S. Yang, 1995. Study of the abzyme with catalytic peroxidase activity. Ann. N. Y. Acad. Sci., 750: 271-276.
  32. Takagi, M., K. Khoda, T. Hamuro, A. Harada, H. Yamaguchi, A. Harada, M. Kamachi and T. Imanaka, 1995. Thermostable peroxidase activity with a recombinant antibody L chainBporphyrin Fe (III) complex. FEBS Lett., 375: 273-276.
  33. Quilez, R., S., de Lauzon, B. Desfosses, D. Mansuy and J.P. Mahy, 1996. Artificial peroxidase-like hemoproteins based on antibodies constructed from a specifically designed ortho-carboxy substituted tetraarylporphyrin hapten and exhibiting a high affinity for iron-porphyrins. FEBS Lett., 395: 73-76.
  34. Kawamura-Konishi, Y., A. Asano, M. Yamasaki, H. Tashiro and H. Suzuki, 1998. Peroxidase activity of an antibodyBferric porphyrin complex. J. Mol. Catal. B: Enzymatic, 4: 181-190.
    Direct Link
  35. Chance, B., 1943. The kinetics of the enzyme-substrate compound of peroxidase. J. Biol. Chem., 151: 553-577.
  36. Ricoux, R., H. Sauriat-Dorizon, E. Girgenti, D. Blanchard and J.P. Mahy, 2002. Hemoabzymes: Towards new biocatalysts for selective oxidations. J. Immunol. Methods, 269: 39-57.
  37. Ricoux, R., E. Girgenti, H. Sauriat-Dorizon, D. Blanchard and J.P. Mahy, 2002. Regioselective nitration of phenol induced by catalytic antibodies. J. Prot. Chem., 21: 473-477.
  38. Ricoux, R., E. Lukowska, F. Pezzotti and J.P. Mahy, 2004. New activities of a catalytic antibody with a peroxidase activity: Formation of Fe (II)-RNO complexes and stereoselective oxidation of sulfides. Eur. J. Biochem., 271: 1277-1283.

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