A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (435 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79953713973&partnerID=40&md5=39abedcde07a73f0f31071229caf1492
Keywords: Bioinorganic Chemistry, Heme Proteins, Michaelis-Menten Kinetics, Peroxidase Activity, Protein Design, Biochemistry, Biomimetics, Catalyst Activity, Enzymes, Hydrogen Peroxide, Oxidation, Peptides, Phenols, Porphyrins, Enzyme Activity, Horseradish Peroxidase, Amino Acid Sequence, Article, Chemical Model, Chemical Structure, Metabolism, Nuclear Magnetic Resonance, Molecular Structure, Biomolecular,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, Complesso Universitario Monte S. Angelo, University of Naples Federico II, Via Cintia, 80126 Naples, Italy
IBB, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Bolon, D.N., Voigt, C.A., Mayo, S.L., (2002) Curr. Opin. Chem. Biol., 6, pp. 125-12
Koder, R.L., Dutton, P.L., (2006) Dalton Trans., pp. 3045-3051
Bolon, D.N., Mayo, S.L., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 14274-14279
Razkin, J., Lindgren, J., Nilsson, H., Baltzer, L., (2008) ChemBioChem, 9, pp. 1975-1984
Jiang, L., (2008) Science, 319, pp. 1387-1391
Röthlisberger, D., (2008) Nature, 453, pp. 190-195
Kaplan, J., Degrado, W.F., (2004) Proc. Natl. Acad. Sci. USA, 101, pp. 11566-11570
Faiella, M., Andreozzi, C., De Rosales, R.T.M., Pavone, V., Maglio, O., Nastri, F., Degrado, W.F., Lombardi, A., (2009) Nat. Chem. Biol., 5, pp. 882-884
Lu, Y., Yeung, N., Sieracki, N., Marshall, N.M., (2009) Nature, 460, pp. 855-862
Lu, Y., (2006) Angew. Chem., 118, pp. 5714-5728
(2006) Angew. Chem. Int. Ed., 45, pp. 5588-5601
Ueno, T., (2010) Angew. Chem., 122, pp. 3958-3959
(2010) Angew. Chem. Int. Ed., 49, pp. 3868-3869
Mansuy, D., (2007) C. R. Chim., 10, pp. 392-413
Tshuva, E.Y., Lippard, S.J., (2004) Chem. Rev., 104, pp. 987-1012
Degrado, W.F., Summa, C.M., Pavone, V., Nastri, F., Lombardi, A., (1999) Ann. Rev. Biochem., 68, pp. 779-819
Lombardi, A., Nastri, F., Pavone, V., (2001) Chem. Rev., 101, pp. 3165-3189
D'auria, G., Maglio, O., Nastri, F., Lombardi, A., Mazzeo, M., Morelli, G., Paolillo, L., Pavone, V., (1997) Chem. Eur. J., 3, pp. 350-362
Di Costanzo, L., Geremia, S., Randaccio, L., Nastri, F., Maglio, O., Lombardi, A., Pavone, V., (2004) J. Biol. Inorg. Chem., 9, pp. 1017-1027
Dunford, H.B., Stillman, J.S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Buchler, J.W., (1979) The Porphyrins, Vol. 1: Structure and Synthesis, pp. 389-483. , (Ed.: D. Dolphin), Academic Press, New York
Munro, O.Q., Marques, H.D., (1996) Inorg. Chem., 35, pp. 3752-3767
Marques, H.D., (2007) Dalton Trans., pp. 4371-4385
Urry, D.W., Pettegrew, J.W., (1967) J. Am. Chem. Soc., 89, pp. 5276-5283
Yonetani, T., Anni, H., (1987) J. Biol. Chem., 262, pp. 9547-9554
Feis, A., Marzocchi, M.P., Paoli, M., Smulevich, G., (1994) Biochemistry, 33, pp. 4577-4583
Yonetani, T., Yamamoto, H., Erman, J.E., Leigh, J.S., Reed, G.H., (1972) J. Biol. Chem., 247, pp. 2447-2455
Adar, F., (1978) The Porphyrins, Vol. 3: Physical Chemistry, , (Ed.: D. Dolphin), Academic Press, New York, Chapter 2
Eaton, W.A., Hofrichter, J., (1981) Methods Enzymol., 76, pp. 175-261
Wittenberg, B.A., Antonini, E., Brunori, M., Noble, R.W., Wittenberg, J.B., Wyman, J., (1967) Biochemistry, 6, pp. 1970-1974
Rossi-Fanelli, A., Antonini, E., (1957) Arch. Biochem. Biophys., 72, pp. 243-246
Adams, P.A., Gold, R.D., (1990) J. Chem. Soc. Chem. Commun., pp. 97-98
Childs, R.E., Bardsley, W.G., (1975) Biochem. J., 145, pp. 93-103
Koduri, R.S., Tien, M., (1995) J. Biol. Chem., 270, pp. 22254-22258
Cleland, W.W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Adams, P.A., (1990) J. Chem. Soc. Perkin Trans. 2, pp. 1407-1414
Savenkova, M.I., Kuo, J.M., Ortiz De Montellano, P.R., (1998) Biochemistry, 37, pp. 10828-10836
Rodriguez-Lopez, J.N., Smith, A.T., Thorneley, R.N.F., (1996) J. Biol. Chem., 271, pp. 4023-4030
Savenkova, M.I., Newmyer, S.L., Ortiz De Montellano, P.R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Ricoux, R., Raffy, Q., Mahy, J.P., (2007) C. R. Chim., 10, pp. 684-702
Sakamoto, S., Sakurai, S., Ueno, A., Mihara, H., (1997) Chem. Commun., pp. 1221-1222
Brunori, M., Amiconi, G., Antonini, E., Wyman, J., Zito, R., Fanelli, A.R., (1968) Biochem. Biophys. Acta Protein Struct., 154, pp. 315-322
Carraway, A.D., McCollum, M.G., Peterson, J., (1996) Inorg. Chem., 35, pp. 6885-6689
Casella, L., Monzani, E., Gullotti, M., De Gioa, L., Strini, A., Chillemi, F., (1996) Inorg. Chem., 35, pp. 439-444
Casella, L., Gullotti, M., De Gioa, L., Monzani, F., Chillemi, F., (1991) J. Chem. Soc. Dalton Trans., pp. 2945-2953
Arnold, P.A., Benson, D.R., Brink, D.J., Hendrich, M.P., Jas, G.S., Kennedy, M.L., Petasis, D.T., Wang, M., (1997) Inorg. Chem., 36, pp. 5306-5315
Benson, D.R., Hart, B.R., Zhu, X., Doughty, M.B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Baldwin, D.A., Marques, H.M., Pratt, J.M., (1986) J. Inorg. Biochem., 27, pp. 245-254
Wilson, M.T., Ranson, R.J., Masiakowski, P., Czarnecka, E., Brunori, M., (1977) Eur. J. Biochem., 77, pp. 193-199
Baldwin, D.A., Mabuya, M.B., Marques, H.M., (1987) S. Afr. J. Chem., 40, p. 103
Budde, C.L., Beyer, A., Munir, I.Z., Dordick, J.S., Khmelnitsky, Y.L., (2001) J. Mol. Catal. B, 15, pp. 55-64
Ricoux, R., Girgenti, E., Sauriant-Dorizon, H., Blanchard, D., Mahy, J.P., (2002) J. Protein Chem., 21, pp. 473-477
Ricoux, R., Boucher, J.L., Mansuy, D., (2001) Eur. J. Biochem., 268, pp. 3783-3788
Dawson, J.H., (1988) Science, 240, pp. 433-439
Barlow, S., Rohl, A.L., Shi, S., Freeman, C.M., O'Hare, D., (1996) J. Am. Chem. Soc., 118, pp. 7578-7592
Wang, J., Araki, T., Matsuoka, M., Ogawa, T., (1999) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1435, pp. 177-183
Bolon, D. N., Voigt, C. A., Mayo, S. L., (2002) Curr. Opin. Chem. Biol., 6, pp. 125-12
Koder, R. L., Dutton, P. L., (2006) Dalton Trans., pp. 3045-3051
Bolon, D. N., Mayo, S. L., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 14274-14279
R thlisberger, D., (2008) Nature, 453, pp. 190-195
Tshuva, E. Y., Lippard, S. J., (2004) Chem. Rev., 104, pp. 987-1012
Degrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., (1999) Ann. Rev. Biochem., 68, pp. 779-819
Dunford, H. B., Stillman, J. S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Buchler, J. W., (1979) The Porphyrins, Vol. 1: Structure and Synthesis, pp. 389-483. , (Ed.: D. Dolphin), Academic Press, New York
Munro, O. Q., Marques, H. D., (1996) Inorg. Chem., 35, pp. 3752-3767
Marques, H. D., (2007) Dalton Trans., pp. 4371-4385
Urry, D. W., Pettegrew, J. W., (1967) J. Am. Chem. Soc., 89, pp. 5276-5283
Eaton, W. A., Hofrichter, J., (1981) Methods Enzymol., 76, pp. 175-261
Wittenberg, B. A., Antonini, E., Brunori, M., Noble, R. W., Wittenberg, J. B., Wyman, J., (1967) Biochemistry, 6, pp. 1970-1974
Adams, P. A., Gold, R. D., (1990) J. Chem. Soc. Chem. Commun., pp. 97-98
Childs, R. E., Bardsley, W. G., (1975) Biochem. J., 145, pp. 93-103
Koduri, R. S., Tien, M., (1995) J. Biol. Chem., 270, pp. 22254-22258
Cleland, W. W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Adams, P. A., (1990) J. Chem. Soc. Perkin Trans. 2, pp. 1407-1414
Savenkova, M. I., Kuo, J. M., Ortiz De Montellano, P. R., (1998) Biochemistry, 37, pp. 10828-10836
Savenkova, M. I., Newmyer, S. L., Ortiz De Montellano, P. R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Carraway, A. D., McCollum, M. G., Peterson, J., (1996) Inorg. Chem., 35, pp. 6885-6689
Arnold, P. A., Benson, D. R., Brink, D. J., Hendrich, M. P., Jas, G. S., Kennedy, M. L., Petasis, D. T., Wang, M., (1997) Inorg. Chem., 36, pp. 5306-5315
Benson, D. R., Hart, B. R., Zhu, X., Doughty, M. B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Baldwin, D. A., Marques, H. M., Pratt, J. M., (1986) J. Inorg. Biochem., 27, pp. 245-254
Wilson, M. T., Ranson, R. J., Masiakowski, P., Czarnecka, E., Brunori, M., (1977) Eur. J. Biochem., 77, pp. 193-199
Baldwin, D. A., Mabuya, M. B., Marques, H. M., (1987) S. Afr. J. Chem., 40, p. 103
Budde, C. L., Beyer, A., Munir, I. Z., Dordick, J. S., Khmelnitsky, Y. L., (2001) J. Mol. Catal. B, 15, pp. 55-64
Dawson, J. H., (1988) Science, 240, pp. 433-439
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79953713973&partnerID=40&md5=39abedcde07a73f0f31071229caf1492
Keywords: Bioinorganic Chemistry, Heme Proteins, Michaelis-Menten Kinetics, Peroxidase Activity, Protein Design, Biochemistry, Biomimetics, Catalyst Activity, Enzymes, Hydrogen Peroxide, Oxidation, Peptides, Phenols, Porphyrins, Enzyme Activity, Horseradish Peroxidase, Amino Acid Sequence, Article, Chemical Model, Chemical Structure, Metabolism, Nuclear Magnetic Resonance, Molecular Structure, Biomolecular,
Affiliations:
*** IBB - CNR ***
Department of Chemistry, Complesso Universitario Monte S. Angelo, University of Naples Federico II, Via Cintia, 80126 Naples, Italy
IBB, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Bolon, D.N., Voigt, C.A., Mayo, S.L., (2002) Curr. Opin. Chem. Biol., 6, pp. 125-12
Koder, R.L., Dutton, P.L., (2006) Dalton Trans., pp. 3045-3051
Bolon, D.N., Mayo, S.L., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 14274-14279
Razkin, J., Lindgren, J., Nilsson, H., Baltzer, L., (2008) ChemBioChem, 9, pp. 1975-1984
Jiang, L., (2008) Science, 319, pp. 1387-1391
Röthlisberger, D., (2008) Nature, 453, pp. 190-195
Kaplan, J., Degrado, W.F., (2004) Proc. Natl. Acad. Sci. USA, 101, pp. 11566-11570
Faiella, M., Andreozzi, C., De Rosales, R.T.M., Pavone, V., Maglio, O., Nastri, F., Degrado, W.F., Lombardi, A., (2009) Nat. Chem. Biol., 5, pp. 882-884
Lu, Y., Yeung, N., Sieracki, N., Marshall, N.M., (2009) Nature, 460, pp. 855-862
Lu, Y., (2006) Angew. Chem., 118, pp. 5714-5728
(2006) Angew. Chem. Int. Ed., 45, pp. 5588-5601
Ueno, T., (2010) Angew. Chem., 122, pp. 3958-3959
(2010) Angew. Chem. Int. Ed., 49, pp. 3868-3869
Mansuy, D., (2007) C. R. Chim., 10, pp. 392-413
Tshuva, E.Y., Lippard, S.J., (2004) Chem. Rev., 104, pp. 987-1012
Degrado, W.F., Summa, C.M., Pavone, V., Nastri, F., Lombardi, A., (1999) Ann. Rev. Biochem., 68, pp. 779-819
Lombardi, A., Nastri, F., Pavone, V., (2001) Chem. Rev., 101, pp. 3165-3189
D'auria, G., Maglio, O., Nastri, F., Lombardi, A., Mazzeo, M., Morelli, G., Paolillo, L., Pavone, V., (1997) Chem. Eur. J., 3, pp. 350-362
Di Costanzo, L., Geremia, S., Randaccio, L., Nastri, F., Maglio, O., Lombardi, A., Pavone, V., (2004) J. Biol. Inorg. Chem., 9, pp. 1017-1027
Dunford, H.B., Stillman, J.S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Buchler, J.W., (1979) The Porphyrins, Vol. 1: Structure and Synthesis, pp. 389-483. , (Ed.: D. Dolphin), Academic Press, New York
Munro, O.Q., Marques, H.D., (1996) Inorg. Chem., 35, pp. 3752-3767
Marques, H.D., (2007) Dalton Trans., pp. 4371-4385
Urry, D.W., Pettegrew, J.W., (1967) J. Am. Chem. Soc., 89, pp. 5276-5283
Yonetani, T., Anni, H., (1987) J. Biol. Chem., 262, pp. 9547-9554
Feis, A., Marzocchi, M.P., Paoli, M., Smulevich, G., (1994) Biochemistry, 33, pp. 4577-4583
Yonetani, T., Yamamoto, H., Erman, J.E., Leigh, J.S., Reed, G.H., (1972) J. Biol. Chem., 247, pp. 2447-2455
Adar, F., (1978) The Porphyrins, Vol. 3: Physical Chemistry, , (Ed.: D. Dolphin), Academic Press, New York, Chapter 2
Eaton, W.A., Hofrichter, J., (1981) Methods Enzymol., 76, pp. 175-261
Wittenberg, B.A., Antonini, E., Brunori, M., Noble, R.W., Wittenberg, J.B., Wyman, J., (1967) Biochemistry, 6, pp. 1970-1974
Rossi-Fanelli, A., Antonini, E., (1957) Arch. Biochem. Biophys., 72, pp. 243-246
Adams, P.A., Gold, R.D., (1990) J. Chem. Soc. Chem. Commun., pp. 97-98
Childs, R.E., Bardsley, W.G., (1975) Biochem. J., 145, pp. 93-103
Koduri, R.S., Tien, M., (1995) J. Biol. Chem., 270, pp. 22254-22258
Cleland, W.W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Adams, P.A., (1990) J. Chem. Soc. Perkin Trans. 2, pp. 1407-1414
Savenkova, M.I., Kuo, J.M., Ortiz De Montellano, P.R., (1998) Biochemistry, 37, pp. 10828-10836
Rodriguez-Lopez, J.N., Smith, A.T., Thorneley, R.N.F., (1996) J. Biol. Chem., 271, pp. 4023-4030
Savenkova, M.I., Newmyer, S.L., Ortiz De Montellano, P.R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Ricoux, R., Raffy, Q., Mahy, J.P., (2007) C. R. Chim., 10, pp. 684-702
Sakamoto, S., Sakurai, S., Ueno, A., Mihara, H., (1997) Chem. Commun., pp. 1221-1222
Brunori, M., Amiconi, G., Antonini, E., Wyman, J., Zito, R., Fanelli, A.R., (1968) Biochem. Biophys. Acta Protein Struct., 154, pp. 315-322
Carraway, A.D., McCollum, M.G., Peterson, J., (1996) Inorg. Chem., 35, pp. 6885-6689
Casella, L., Monzani, E., Gullotti, M., De Gioa, L., Strini, A., Chillemi, F., (1996) Inorg. Chem., 35, pp. 439-444
Casella, L., Gullotti, M., De Gioa, L., Monzani, F., Chillemi, F., (1991) J. Chem. Soc. Dalton Trans., pp. 2945-2953
Arnold, P.A., Benson, D.R., Brink, D.J., Hendrich, M.P., Jas, G.S., Kennedy, M.L., Petasis, D.T., Wang, M., (1997) Inorg. Chem., 36, pp. 5306-5315
Benson, D.R., Hart, B.R., Zhu, X., Doughty, M.B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Baldwin, D.A., Marques, H.M., Pratt, J.M., (1986) J. Inorg. Biochem., 27, pp. 245-254
Wilson, M.T., Ranson, R.J., Masiakowski, P., Czarnecka, E., Brunori, M., (1977) Eur. J. Biochem., 77, pp. 193-199
Baldwin, D.A., Mabuya, M.B., Marques, H.M., (1987) S. Afr. J. Chem., 40, p. 103
Budde, C.L., Beyer, A., Munir, I.Z., Dordick, J.S., Khmelnitsky, Y.L., (2001) J. Mol. Catal. B, 15, pp. 55-64
Ricoux, R., Girgenti, E., Sauriant-Dorizon, H., Blanchard, D., Mahy, J.P., (2002) J. Protein Chem., 21, pp. 473-477
Ricoux, R., Boucher, J.L., Mansuy, D., (2001) Eur. J. Biochem., 268, pp. 3783-3788
Dawson, J.H., (1988) Science, 240, pp. 433-439
Barlow, S., Rohl, A.L., Shi, S., Freeman, C.M., O'Hare, D., (1996) J. Am. Chem. Soc., 118, pp. 7578-7592
Wang, J., Araki, T., Matsuoka, M., Ogawa, T., (1999) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1435, pp. 177-183
Bolon, D. N., Voigt, C. A., Mayo, S. L., (2002) Curr. Opin. Chem. Biol., 6, pp. 125-12
Koder, R. L., Dutton, P. L., (2006) Dalton Trans., pp. 3045-3051
Bolon, D. N., Mayo, S. L., (2001) Proc. Natl. Acad. Sci. USA, 98, pp. 14274-14279
R thlisberger, D., (2008) Nature, 453, pp. 190-195
Tshuva, E. Y., Lippard, S. J., (2004) Chem. Rev., 104, pp. 987-1012
Degrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., (1999) Ann. Rev. Biochem., 68, pp. 779-819
Dunford, H. B., Stillman, J. S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Buchler, J. W., (1979) The Porphyrins, Vol. 1: Structure and Synthesis, pp. 389-483. , (Ed.: D. Dolphin), Academic Press, New York
Munro, O. Q., Marques, H. D., (1996) Inorg. Chem., 35, pp. 3752-3767
Marques, H. D., (2007) Dalton Trans., pp. 4371-4385
Urry, D. W., Pettegrew, J. W., (1967) J. Am. Chem. Soc., 89, pp. 5276-5283
Eaton, W. A., Hofrichter, J., (1981) Methods Enzymol., 76, pp. 175-261
Wittenberg, B. A., Antonini, E., Brunori, M., Noble, R. W., Wittenberg, J. B., Wyman, J., (1967) Biochemistry, 6, pp. 1970-1974
Adams, P. A., Gold, R. D., (1990) J. Chem. Soc. Chem. Commun., pp. 97-98
Childs, R. E., Bardsley, W. G., (1975) Biochem. J., 145, pp. 93-103
Koduri, R. S., Tien, M., (1995) J. Biol. Chem., 270, pp. 22254-22258
Cleland, W. W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Adams, P. A., (1990) J. Chem. Soc. Perkin Trans. 2, pp. 1407-1414
Savenkova, M. I., Kuo, J. M., Ortiz De Montellano, P. R., (1998) Biochemistry, 37, pp. 10828-10836
Savenkova, M. I., Newmyer, S. L., Ortiz De Montellano, P. R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Carraway, A. D., McCollum, M. G., Peterson, J., (1996) Inorg. Chem., 35, pp. 6885-6689
Arnold, P. A., Benson, D. R., Brink, D. J., Hendrich, M. P., Jas, G. S., Kennedy, M. L., Petasis, D. T., Wang, M., (1997) Inorg. Chem., 36, pp. 5306-5315
Benson, D. R., Hart, B. R., Zhu, X., Doughty, M. B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Baldwin, D. A., Marques, H. M., Pratt, J. M., (1986) J. Inorg. Biochem., 27, pp. 245-254
Wilson, M. T., Ranson, R. J., Masiakowski, P., Czarnecka, E., Brunori, M., (1977) Eur. J. Biochem., 77, pp. 193-199
Baldwin, D. A., Mabuya, M. B., Marques, H. M., (1987) S. Afr. J. Chem., 40, p. 103
Budde, C. L., Beyer, A., Munir, I. Z., Dordick, J. S., Khmelnitsky, Y. L., (2001) J. Mol. Catal. B, 15, pp. 55-64
Dawson, J. H., (1988) Science, 240, pp. 433-439
A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity
Mimicking enzymes with alternative molecules represents an important objective in synthetic biology, aimed to obtain new chemical entities for specific applications. This objective is hampered by the large size and complexity of enzymes. The manipulation of their structures often leads to a reduction of enzyme activity. Herein, we describe the spectroscopic and functional characterization of Fe(III)-mimochrome VI, a 3.5 kDa synthetic hemeprotein model, which displays a peroxidase-like catalytic activity. By the use of hydrogen peroxide, Fe(III)-mimochrome VI efficiently catalyzes the oxidation of several substrates, with a typical Michaelis-Menten mechanism and with several multiple turnovers. The catalytic efficiency of Fe(III)-mimochrome VI in the oxidation of 2,2'-azino-di(3-ethyl-benzothiazoline-6-sulfonic acid (ABTS) and guaiacol (k(cat)/K(m)=4417 and 870 mM(-1)s(-1), respectively) is comparable to that of native horseradish peroxidase (HRP, k(cat)/K(m)=5125 and 500 mM(-1)s(-1), respectively). Fe(III)-mimochrome VI also converts phenol to 4- and 2-nitrophenol in the presence of NO(2)(-) and H(2)O(2) in high yields. These results demonstrate that small synthetic peptides can impart high enzyme activities to metal cofactors, and anticipate the possibility of constructing new biocatalysts tailored to specific functions.
Mimicking enzymes with alternative molecules represents an important objective in synthetic biology, aimed to obtain new chemical entities for specific applications. This objective is hampered by the large size and complexity of enzymes. The manipulation of their structures often leads to a reduction of enzyme activity. Herein, we describe the spectroscopic and functional characterization of Fe(III)-mimochrome VI, a 3.5 kDa synthetic hemeprotein model, which displays a peroxidase-like catalytic activity. By the use of hydrogen peroxide, Fe(III)-mimochrome VI efficiently catalyzes the oxidation of several substrates, with a typical Michaelis-Menten mechanism and with several multiple turnovers. The catalytic efficiency of Fe(III)-mimochrome VI in the oxidation of 2,2'-azino-di(3-ethyl-benzothiazoline-6-sulfonic acid (ABTS) and guaiacol (k(cat)/K(m)=4417 and 870 mM(-1)s(-1), respectively) is comparable to that of native horseradish peroxidase (HRP, k(cat)/K(m)=5125 and 500 mM(-1)s(-1), respectively). Fe(III)-mimochrome VI also converts phenol to 4- and 2-nitrophenol in the presence of NO(2)(-) and H(2)O(2) in high yields. These results demonstrate that small synthetic peptides can impart high enzyme activities to metal cofactors, and anticipate the possibility of constructing new biocatalysts tailored to specific functions.
A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity
| ▼ Syntethic metalloproteins and peptides for biosensing applications |
A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity
Other filter: ([btitle,keywords] "Bioinorganic Chemist ...
Chino M, Zhang SQ, Pirro F, Leone L, Maglio O, Lombardi A, Degrado WF
* Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster (315 views)
Biopolymers (ISSN: 1097-0282electronic, 0006-3525linking, 0006-3525print), 2018 Sep 11; 109(10): e23339-e23339.
Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Chino M, Leone L, Zambrano G, Pirro F, D'Alonzo D, Firpo V, Aref D, Lista L, Maglio O, Nastri F, Lombardi A
* Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages (239 views)
Biopolymers (ISSN: 0006-3525linking, 0006-3525print, 1097-0282electronic), 2018 Aug; 109(10): e23107-e23107.
Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Caserta G, Chino M, Firpo V, Zambrano G, Leone L, D'Alonzo D, Nastri F, Maglio O, Pavone V, Lombardi A
* Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design (266 views)
Chembiochem, 2018; 19: 1823-1826.
Impact Factor: 2.774
View Export to BibTeX Export to EndNote
Chino M, Leone L, Maglio O, D'Alonzo D, Pirro F, Pavone V, Nastri F, Lombardi A
* A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation (246 views) (PDF 169 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2017 Dec 4; 56(49): 15580-15583.
Impact Factor: 12.102
View Export to BibTeX Export to EndNote
Messori L, Merlino A
* Cisplatin binding to proteins: A structural perspective (421 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 315: 67-89.
Impact Factor: 13.324
View Export to BibTeX Export to EndNote
Trusso Sfrazzetto G, Satriano C, Tomaselli GA, Rizzarelli E
* Synthetic fluorescent probes to map metallostasis and intracellular fate of zinc and copper (330 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 311: 125-167.
Impact Factor: 13.324
View Export to BibTeX Export to EndNote
Chino M, Maglio O, Nastri F, Pavone V, Degrado WF, Lombardi A
* Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (563 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
Impact Factor: 2.686
View Export to BibTeX Export to EndNote
Faiella M, Maglio O, Nastri F, Lombardi A, Lista L, Hagen WR, Pavone V
* De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (474 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2012 Dec 7; 18(50): 15960-15971.
Impact Factor: 5.831
View Export to BibTeX Export to EndNote
Maglio O, Nastri F, Lombardi A, Ciferri A, Perico A
* Structural and Functional Aspects of Metal Binding Sites in Natural and Designed Metalloproteins (535 views)
Ionic Interactions In Nat And Synthetic Macromolecules John Wiley And Sons (ISSN: 9780-4705), 2012; N/D: 361-450.
Impact Factor: 5.927
View Export to BibTeX Export to EndNote
Kállay C, Turi I, Timári S, Nagy Z, Sanna D, Pappalardo G, De Bona P, Rizzarelli E, Sóvágó I
* The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein (503 views)
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
Impact Factor: 1.532
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (461 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, Degrado WF
* Analysis and design of turns in α-helical hairpins (471 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005; 346(5): 1441-1454.
Impact Factor: 5.229
View Export to BibTeX Export to EndNote
Calhoun JR, Nastri F, Maglio O, Pavone V, Lombardi A, Degrado WF
* Artificial diiron proteins: From structure to function (480 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005; 80(2-3): 264-278.
Impact Factor: 2.545
View Export to BibTeX Export to EndNote
Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (378 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
View Export to BibTeX Export to EndNote
Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (534 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
View Export to BibTeX Export to EndNote
Main ERG, Xiong Y, Cocco MJ, D'Andrea LD, Regan L
* Design of stable α-helical arrays from an idealized TPR motif (925 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2003; 11(5): 497-508.
Impact Factor: 5.993
View Export to BibTeX Export to EndNote
Nastri F, Lombardi A, Morelli G, Maglio O, D'Auria G, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (536 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 2. Structural characterization of Co(III) mimochrome I Δ and Λ isomers (486 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
Pacelli R, Taira J, Cook JA, Wink DA, Krishna MC
Hydroxyurea reacts with heme proteins to generate nitric oxide [6] (334 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
View Export to BibTeX Export to EndNote
* Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster (315 views)
Biopolymers (ISSN: 1097-0282electronic, 0006-3525linking, 0006-3525print), 2018 Sep 11; 109(10): e23339-e23339.
Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Chino M, Leone L, Zambrano G, Pirro F, D'Alonzo D, Firpo V, Aref D, Lista L, Maglio O, Nastri F, Lombardi A
* Oxidation catalysis by iron and manganese porphyrins within enzyme-like cages (239 views)
Biopolymers (ISSN: 0006-3525linking, 0006-3525print, 1097-0282electronic), 2018 Aug; 109(10): e23107-e23107.
Impact Factor: 2.572
View Export to BibTeX Export to EndNote
Caserta G, Chino M, Firpo V, Zambrano G, Leone L, D'Alonzo D, Nastri F, Maglio O, Pavone V, Lombardi A
* Enhancement of Peroxidase Activity in Artificial Mimochrome VI Catalysts through Rational Design (266 views)
Chembiochem, 2018; 19: 1823-1826.
Impact Factor: 2.774
View Export to BibTeX Export to EndNote
Chino M, Leone L, Maglio O, D'Alonzo D, Pirro F, Pavone V, Nastri F, Lombardi A
* A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation (246 views) (PDF 169 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2017 Dec 4; 56(49): 15580-15583.
Impact Factor: 12.102
View Export to BibTeX Export to EndNote
Messori L, Merlino A
* Cisplatin binding to proteins: A structural perspective (421 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 315: 67-89.
Impact Factor: 13.324
View Export to BibTeX Export to EndNote
Trusso Sfrazzetto G, Satriano C, Tomaselli GA, Rizzarelli E
* Synthetic fluorescent probes to map metallostasis and intracellular fate of zinc and copper (330 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 311: 125-167.
Impact Factor: 13.324
View Export to BibTeX Export to EndNote
Chino M, Maglio O, Nastri F, Pavone V, Degrado WF, Lombardi A
* Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (563 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
Impact Factor: 2.686
View Export to BibTeX Export to EndNote
Faiella M, Maglio O, Nastri F, Lombardi A, Lista L, Hagen WR, Pavone V
* De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (474 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2012 Dec 7; 18(50): 15960-15971.
Impact Factor: 5.831
View Export to BibTeX Export to EndNote
Maglio O, Nastri F, Lombardi A, Ciferri A, Perico A
* Structural and Functional Aspects of Metal Binding Sites in Natural and Designed Metalloproteins (535 views)
Ionic Interactions In Nat And Synthetic Macromolecules John Wiley And Sons (ISSN: 9780-4705), 2012; N/D: 361-450.
Impact Factor: 5.927
View Export to BibTeX Export to EndNote
Kállay C, Turi I, Timári S, Nagy Z, Sanna D, Pappalardo G, De Bona P, Rizzarelli E, Sóvágó I
* The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein (503 views)
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
Impact Factor: 1.532
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Scarabelli G, Pedone C, Colombo G, D'Andrea LD, Fattorusso R
* Structural analysis of a helical peptide unfolding pathway (461 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2010 May 10; 16(18): 5400-5407.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Lahr SJ, Engel DE, Stayrook SE, Maglio O, North B, Geremia S, Lombardi A, Degrado WF
* Analysis and design of turns in α-helical hairpins (471 views)
J Mol Biol (ISSN: 0022-2836, 1089-8638, 1089-8638electronic), 2005; 346(5): 1441-1454.
Impact Factor: 5.229
View Export to BibTeX Export to EndNote
Calhoun JR, Nastri F, Maglio O, Pavone V, Lombardi A, Degrado WF
* Artificial diiron proteins: From structure to function (480 views)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2005; 80(2-3): 264-278.
Impact Factor: 2.545
View Export to BibTeX Export to EndNote
Di Costanzo L, Geremia S, Randaccio L, Nastri F, Maglio O, Lombardi A, Pavone V
* Miniaturized heme proteins: crystal structure of Co(III)-mimochrome IV (378 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
View Export to BibTeX Export to EndNote
Lombardi A, Nastri F, Marasco D, Maglio O, De Sanctis G, Sinibaldi F, Santucci R, Coletta M, Pavone V
* Design of a new mimochrome with unique topology (534 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2003 Nov 21; 9(22): 5643-5654.
Impact Factor: 4.353
View Export to BibTeX Export to EndNote
Main ERG, Xiong Y, Cocco MJ, D'Andrea LD, Regan L
* Design of stable α-helical arrays from an idealized TPR motif (925 views)
Structure (ISSN: 0969-2126, 1878-4186, 0969-2126linking), 2003; 11(5): 497-508.
Impact Factor: 5.993
View Export to BibTeX Export to EndNote
Nastri F, Lombardi A, Morelli G, Maglio O, D'Auria G, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (536 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
D'Auria G, Maglio O, Nastri F, Lombardi A, Mazzeo M, Morelli G, Paolillo L, Pedone C, Pavone V
Hemoprotein models based on a covalent helix-heme-helix sandwich: 2. Structural characterization of Co(III) mimochrome I Δ and Λ isomers (486 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 350-362.
Impact Factor: 4.828
View Export to BibTeX Export to EndNote
Pacelli R, Taira J, Cook JA, Wink DA, Krishna MC
Hydroxyurea reacts with heme proteins to generate nitric oxide [6] (334 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
View Export to BibTeX Export to EndNote
19 Records (18 excluding Abstracts).
Total impact factor: 115.331 (99.196 excluding Abstracts).
Total 5 year impact factor: 119.524 (95.323 excluding Abstracts).
Total impact factor: 115.331 (99.196 excluding Abstracts).
Total 5 year impact factor: 119.524 (95.323 excluding Abstracts).
435 views. Last view on Wednesday 22 February 2023, 7:44:10
ibb.cnr.it
