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.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.831, 5-year impact factor: 5.623
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84870575652&partnerID=40&md5=e9c73d77587b85338d755932dcf70809
Keywords: Bioinorganic Chemistry, Enzyme Models, Four-Helix Bundles, Peroxidase Activity, Protein Design, Peroxidase Activities, Biochemistry, Biomimetics, Experiments, Hydrogen Peroxide, Iron Compounds, Ligands, Metal Ions, Peptides, Scaffolds (biology), Ferric Ion, Hemoprotein, Metalloprotein, Amino Acid Sequence, Article, Binding Site, Catalysis, Chemical Model, Circular Dichroism, Kinetics, Metabolism, Oxidation Reduction Reaction, Protein Engineering, Protein Secondary Structure, Synthesis, Ultraviolet Spectrophotometry, Ferric Compounds, Hemeproteins, Oxidation-Reduction, Protein Structure,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, Complesso Universitario Monte S. Angelo, University of Naples Federico II, Via Cintia, 80126 Naples, Italy
Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, Netherlands
IBB, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Montellano, P.R.O.D., (2004) Cytochrome P450: Structure, Mechanism, and Biochemistry, p. 689. , 3 rd ed., Kluwer Academic/Plenum Publishers, New York,
Meunier, B., De Visser, S.P., Shaik, S., (2004) Chem. Rev., 104, pp. 3947-3980
Morris, D.L., Hager, L.P., (1966) J. Biol. Chem., 241, pp. 1763-1768
Sundaramoorthy, M., Terner, J., Poulos, T.L., (1995) Structure, 3, pp. 1367-1377
Perutz, M.F., Muirhead, H., Cox, J.M., Goaman, L.C.G., Mathews, F.S., McGandy, E.L., Webb, L.E., (1968) Nature, 219, pp. 29-32
Shikama, K., (1998) Chem. Rev., 98, pp. 1357-1373
Van Deurzen, M.P.J.V., Rantwijk, F.V., Sheldon, R.A., (1997) Tetrahedron, 53, pp. 13183-13220
Veitch, N.C., (2004) Phytochemistry, 65, pp. 249-259
Lu, Y., Yeung, N., Sieracki, N., Marshall, N.M., (2009) Nature, 460, pp. 855-862
Nanda, V., Koder, R.L., (2010) Nat. Chem., 2, pp. 15-24
Smith, B.A., Hecht, M.H., (2011) Curr. Opin. Chem. Biol., 15, pp. 421-426
Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M., Hecht, M.H., (1993) Science, 262, pp. 1680-1685
Koder, R.L., Anderson, J.L., Solomon, L.A., Reddy, K.S., Moser, C.C., Dutton, P.L., (2009) Nature, 458, pp. 305-309
Ghirlanda, G., Osyczka, A., Liu, W., Antolovich, M., Smith, K.M., Dutton, P.L., Wand, A.J., Degrado, W.F., (2004) J. Am. Chem. Soc., 126, pp. 8141-8147
Gibney, B.R., Huang, S.S., Skalicky, J.J., Fuentes, E.J., Wand, A.J., Dutton, P.L., (2001) Biochemistry, 40, pp. 10550-10561
Benson, D.R., Hart, B.R., Zhu, X., Doughty, M.B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Robertson, D.E., Farid, R.S., Moser, C.C., Urbauer, J.L., Mulholland, S.E., Pidikiti, R., Lear, J.D., Dutton, P.L., (1994) Nature, 368, pp. 425-432
Ishida, M., Dohmae, N., Shiro, Y., Oku, T., Iizuka, T., Isogai, Y., (2004) Biochemistry, 43, pp. 9823-9833
Monien, B.H., Drepper, F., Sommerhalter, M., Lubitz, W., Haehnel, W., (2007) J. Mol. Biol., 371, pp. 739-753
Nastri, F., Lista, L., Ringhieri, P., Vitale, R., Faiella, M., Andreozzi, C., Travascio, P., Pavone, V., (2011) Chem. Eur. J., 17, pp. 4444-4453
Zhuang, J., Amoroso, J.H., Kinloch, R., Dawson, J.H., Baldwin, M.J., Gibney, B.R., (2004) Inorg. Chem., 43, pp. 8218-8220
Wei, Y., Kim, S., Fela, D., Baum, J., Hecht, M.H., (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 13270-13273
Wei, Y., Liu, T., Sazinsky, S.L., Moffet, D.A., Pelczer, I., Hecht, M.H., (2003) Protein Sci., 12, pp. 92-102
Moffet, D.A., Case, M.A., House, J.C., Vogel, K., Williams, R.D., Spiro, T.G., McLendon, G.L., Hecht, M.H., (2001) J. Am. Chem. Soc., 123, pp. 2109-2115
Das, A., Hecht, M.H., (2007) J. Inorg. Biochem., 101, pp. 1820-1826
Frolow, F., Kalb, A.J., Yariv, J., (1994) Nat. Struct. Biol., 1, pp. 453-460
Aurora, R., Srinivasan, R., Rose, G.D., (1994) Science, 264, pp. 1126-1130
Lahr, S.J., Engel, D.E., Stayrook, S.E., Maglio, O., North, B., Geremia, S., Lombardi, A., Degrado, W.F., (2005) J. Mol. Biol., 346, pp. 1441-1454
Aurora, R., Rose, G.D., (1998) Protein Sci., 7, pp. 21-38
Richardson, J.S., Richardson, D.C., (1988) Science, 240, pp. 1648-1652
Doig, A.J., Baldwin, R.L., (1995) Protein Sci., 4, pp. 1325-1335
Buchler, J.W., (1979) The Porphyrins, Vol. 1, Structure and Synthesis, Part A, pp. 389-483. , in (Ed.: D. Dolphin), Academic Press, New York
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
Greenfield, N.J., Fasman, G.D., (1969) Biochemistry, 8, pp. 4108-4116
Perez-Iratxeta, C., Andrade-Navarro, M.A., (2008) BMC Struct. Biol., 8, pp. 25-29
Makinen, M.W., Churg, A.K., (1983) Physical Bioinorganic Chemistry, Vol. 1, Iron Porphyrins, Part i, pp. 141-235. , in (Eds.: A. B. P. Lever, H. B. Gray), Addison-Wesley, Reading
Feis, A., Marzocchi, M.P., Paoli, M., Smulevich, G., (1994) Biochemistry, 33, pp. 4577-4583
Kennedy, M.L., Silchenko, S., Houndonougbo, N., Gibney, B.R., Dutton, P.L., Rodgers, K.R., Benson, D.R., (2001) J. Am. Chem. Soc., 123, pp. 4635-4636
Blumberg, W.E., Peisach, J., Wittenberg, B.A., Wittenberg, J.B., (1968) J. Biol. Chem., 243, pp. 1854-1862
Vickery, L., Nozawa, T., Sauer, K., (1976) J. Am. Chem. Soc., 98, pp. 343-350
Kobayashi, N., Tsunenori, N., Hatano, M., (1977) Biochim. Biophys. Acta Protein Struct., 493, pp. 340-351
Nozawa, T., Kobayashi, N., Hatano, M., (1976) Biochim. Biophys. Acta Protein Struct., 427, pp. 652-662
Degrado, W.F., Summa, C.M., Pavone, V., Nastri, F., Lombardi, A., (1999) Annu. Rev. Biochem., 68, pp. 779-819
Wang, J., Araki, T., Matsuoka, M., Ogawa, T., (1999) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1435, pp. 177-183
Sakamoto, S., Sakurai, S., Ueno, A., Mihara, H., (1997) Chem. Commun., pp. 1221-1222
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., Montellano, P.R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Mahy, J.-P., Raffy, Q., Allard, M., Ricoux, R., (2009) Biochimie, 91, pp. 1321-1323
Ricoux, R., Raffy, Q., Mahy, J.-P., (2007) C. R. Chim., 10, pp. 684-702
De Lauzon, S., Mansuy, D., Mahy, J.-P., (2002) Eur. J. Biochem., 269, pp. 470-480
Romesberg, F.E., Santarsiero, B.D., Spiller, B., Yin, J., Barnes, D., Schultz, P.G., Stevens, R.C., (1998) Biochemistry, 37, pp. 14404-14409
De Lauzon, S., Quilez, R., Lion, L., Desfosses, B., Desfosses, B., Lee, I., Sari, M.-A., Mahy, J.-P., (1998) Eur. J. Biochem., 257, pp. 121-130
De Lauzon, S., Desfosses, B., Mansuy, D., Mahy, J.-P., (1999) FEBS Lett., 443, pp. 229-234
Kunishima, N., Amada, F., Fukuyama, K., Kawamoto, M., Matsunaga, T., Matsubara, H., (1996) FEBS Lett., 378, pp. 291-294
Pond, A.E., Sono, M., Elenkova, E.A., McRee, D.E., Goodin, D.B., English, A.M., Dawson, J.H., (1999) J. Inorg. Biochem., 76, pp. 165-174
Suzuki, S., (1991) J. Inorg. Biochem., 44, pp. 267-276
Howes, B.D., Rodriguez-Lopez, J.N., Smith, A.T., Smulevich, G., (1997) Biochemistry, 36, pp. 1532-1543
Marques, H.M., (2007) Dalton Trans., pp. 4371-4385
Matthew, J.B., (1985) Ann. Rev. Biophys. Biophys. Chem., 14, pp. 387-417
Dawson, J.H., Dooley, D.M., (1989) Physical Bioinorganic Chemistry, Vol. 4, Iron Porphyrins, Part III, pp. 1-136. , in (Eds.: A. B. P. Lever, H. B. Gray), VCH, New York
Neri, F., Kok, D., Miller, M.A., Smulevich, G., (1997) Biochemistry, 36, pp. 8947-8953
Asakura, T., Reed, G.H., Leigh, J.S., (1972) Biochemistry, 11, pp. 334-338
Dunford, H.B., Stillman, J.S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Poulos, T.L., Kraut, J., (1980) J. Biol. Chem., 255, pp. 8199-8205
Erman, J.E., Vitello, L.B., Miller, M.A., Shaw, A., Brown, K.A., Kraut, J., (1993) Biochemistry, 32, pp. 9798-9806
Newmyer, S.L., De Montellano, P.R.O., (1995) J. Biol. Chem., 270, pp. 19430-19438
Rodríguez-López, J.N., Lowe, D.J., Hernández-Ruiz, J., Hiner, A.N.P., García-Cánovas, F., Thorneley, R.N.F., (2001) J. Am. Chem. Soc., 123, pp. 11838-11847
Vitello, L.B., Erman, J.E., Miller, M.A., Wang, J., Kraut, J., (1993) Biochemistry, 32, pp. 9807-9818
Dawson, J.H., Sono, M., (1987) Chem. Rev., 87, pp. 1255-1276
Dolphin, D., Forman, A., Borg, D.C., Fajer, J., Felton, R.H., (1971) Proc. Natl. Acad. Sci. USA, 68, pp. 614-618
Schonbaum, G.R., Lo, S., (1972) J. Biol. Chem., 247, pp. 3353-3360
Dunford, H.B., (1991) Peroxidases in Chemistry and Biology, Vol. 2, pp. 1-24. , in (Eds.: J. Everse, K. E. Everse, M. B. Grisham), CRC Press, Boca Raton
Egawa, T., Shimada, H., Ishimura, Y., (2000) J. Biol. Chem., 275, pp. 34858-34866
Matsui, T., Ozaki S.-I, Liong, E., Phillips, G.N., Watanabe, Y., (1999) J. Biol. Chem., 274, pp. 2838-2844
Fox, J.B., Nicholas, R.A., Ackerman, S.A., Swift, C.E., (1974) Biochemistry, 13, pp. 5178-5186
English, A.M., Tsaprailis, G., (1995) Adv. Inorg. Chem., 43, pp. 79-125
Allentoff, A.J., Bolton, J.L., Wilks, A., Thompson, J.A., Ortiz De Montellano, P.R., (1992) J. Am. Chem. Soc., 114, pp. 9744-9749
Barlow, S., Rohl, A.L., Shi, S., Freeman, C.M., O'Hare, D., (1996) J. Am. Chem. Soc., 118, pp. 7578-7592
Childs, B.R.E., Bardsley, W.G., (1975) Biochem. J., 145, pp. 93-103
Cleland, W.W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Takakuwa, T., Konno, T., Meguro, H., (1985) Anal. Sci., 1, pp. 215-218
Holmquist, B., (1986) Methods Enzymol., 130, pp. 270-290
Montellano, P. R. O. D., (2004) Cytochrome P450: Structure, Mechanism, and Biochemistry, p. 689. , 3 rd ed., Kluwer Academic/Plenum Publishers, New York,
Morris, D. L., Hager, L. P., (1966) J. Biol. Chem., 241, pp. 1763-1768
Perutz, M. F., Muirhead, H., Cox, J. M., Goaman, L. C. G., Mathews, F. S., McGandy, E. L., Webb, L. E., (1968) Nature, 219, pp. 29-32
Van Deurzen, M. P. J. V., Rantwijk, F. V., Sheldon, R. A., (1997) Tetrahedron, 53, pp. 13183-13220
Veitch, N. C., (2004) Phytochemistry, 65, pp. 249-259
Smith, B. A., Hecht, M. H., (2011) Curr. Opin. Chem. Biol., 15, pp. 421-426
Koder, R. L., Anderson, J. L., Solomon, L. A., Reddy, K. S., Moser, C. C., Dutton, P. L., (2009) Nature, 458, pp. 305-309
Gibney, B. R., Huang, S. S., Skalicky, J. J., Fuentes, E. J., Wand, A. J., Dutton, P. L., (2001) Biochemistry, 40, pp. 10550-10561
Benson, D. R., Hart, B. R., Zhu, X., Doughty, M. B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Robertson, D. E., Farid, R. S., Moser, C. C., Urbauer, J. L., Mulholland, S. E., Pidikiti, R., Lear, J. D., Dutton, P. L., (1994) Nature, 368, pp. 425-432
Monien, B. H., Drepper, F., Sommerhalter, M., Lubitz, W., Haehnel, W., (2007) J. Mol. Biol., 371, pp. 739-753
Moffet, D. A., Case, M. A., House, J. C., Vogel, K., Williams, R. D., Spiro, T. G., McLendon, G. L., Hecht, M. H., (2001) J. Am. Chem. Soc., 123, pp. 2109-2115
Das, A., Hecht, M. H., (2007) J. Inorg. Biochem., 101, pp. 1820-1826
Lahr, S. J., Engel, D. E., Stayrook, S. E., Maglio, O., North, B., Geremia, S., Lombardi, A., Degrado, W. F., (2005) J. Mol. Biol., 346, pp. 1441-1454
Richardson, J. S., Richardson, D. C., (1988) Science, 240, pp. 1648-1652
Doig, A. J., Baldwin, R. L., (1995) Protein Sci., 4, pp. 1325-1335
Buchler, J. W., (1979) The Porphyrins, Vol. 1, Structure and Synthesis, Part A, pp. 389-483. , in (Ed.: D. Dolphin), Academic Press, New York
Greenfield, N. J., Fasman, G. D., (1969) Biochemistry, 8, pp. 4108-4116
Makinen, M. W., Churg, A. K., (1983) Physical Bioinorganic Chemistry, Vol. 1, Iron Porphyrins, Part i, pp. 141-235. , in (Eds.: A. B. P. Lever, H. B. Gray), Addison-Wesley, Reading
Kennedy, M. L., Silchenko, S., Houndonougbo, N., Gibney, B. R., Dutton, P. L., Rodgers, K. R., Benson, D. R., (2001) J. Am. Chem. Soc., 123, pp. 4635-4636
Blumberg, W. E., Peisach, J., Wittenberg, B. A., Wittenberg, J. B., (1968) J. Biol. Chem., 243, pp. 1854-1862
Degrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., (1999) Annu. Rev. Biochem., 68, pp. 779-819
Savenkova, M. I., Kuo, J. M., Ortiz De Montellano, P. R., (1998) Biochemistry, 37, pp. 10828-10836
Savenkova, M. I., Newmyer, S. L., Montellano, P. R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Mahy, J. -P., Raffy, Q., Allard, M., Ricoux, R., (2009) Biochimie, 91, pp. 1321-1323
Romesberg, F. E., Santarsiero, B. D., Spiller, B., Yin, J., Barnes, D., Schultz, P. G., Stevens, R. C., (1998) Biochemistry, 37, pp. 14404-14409
Pond, A. E., Sono, M., Elenkova, E. A., McRee, D. E., Goodin, D. B., English, A. M., Dawson, J. H., (1999) J. Inorg. Biochem., 76, pp. 165-174
Howes, B. D., Rodriguez-Lopez, J. N., Smith, A. T., Smulevich, G., (1997) Biochemistry, 36, pp. 1532-1543
Marques, H. M., (2007) Dalton Trans., pp. 4371-4385
Matthew, J. B., (1985) Ann. Rev. Biophys. Biophys. Chem., 14, pp. 387-417
Dawson, J. H., Dooley, D. M., (1989) Physical Bioinorganic Chemistry, Vol. 4, Iron Porphyrins, Part III, pp. 1-136. , in (Eds.: A. B. P. Lever, H. B. Gray), VCH, New York
Dunford, H. B., Stillman, J. S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Poulos, T. L., Kraut, J., (1980) J. Biol. Chem., 255, pp. 8199-8205
Erman, J. E., Vitello, L. B., Miller, M. A., Shaw, A., Brown, K. A., Kraut, J., (1993) Biochemistry, 32, pp. 9798-9806
Newmyer, S. L., De Montellano, P. R. O., (1995) J. Biol. Chem., 270, pp. 19430-19438
Rodr guez-L pez, J. N., Lowe, D. J., Hern ndez-Ruiz, J., Hiner, A. N. P., Garc a-C novas, F., Thorneley, R. N. F., (2001) J. Am. Chem. Soc., 123, pp. 11838-11847
Vitello, L. B., Erman, J. E., Miller, M. A., Wang, J., Kraut, J., (1993) Biochemistry, 32, pp. 9807-9818
Dawson, J. H., Sono, M., (1987) Chem. Rev., 87, pp. 1255-1276
Schonbaum, G. R., Lo, S., (1972) J. Biol. Chem., 247, pp. 3353-3360
Dunford, H. B., (1991) Peroxidases in Chemistry and Biology, Vol. 2, pp. 1-24. , in (Eds.: J. Everse, K. E. Everse, M. B. Grisham), CRC Press, Boca Raton
Fox, J. B., Nicholas, R. A., Ackerman, S. A., Swift, C. E., (1974) Biochemistry, 13, pp. 5178-5186
English, A. M., Tsaprailis, G., (1995) Adv. Inorg. Chem., 43, pp. 79-125
Allentoff, A. J., Bolton, J. L., Wilks, A., Thompson, J. A., Ortiz De Montellano, P. R., (1992) J. Am. Chem. Soc., 114, pp. 9744-9749
Childs, B. R. E., Bardsley, W. G., (1975) Biochem. J., 145, pp. 93-103
Cleland, W. W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2012 Dec 7; 18(50): 15960-15971.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 5.831, 5-year impact factor: 5.623
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84870575652&partnerID=40&md5=e9c73d77587b85338d755932dcf70809
Keywords: Bioinorganic Chemistry, Enzyme Models, Four-Helix Bundles, Peroxidase Activity, Protein Design, Peroxidase Activities, Biochemistry, Biomimetics, Experiments, Hydrogen Peroxide, Iron Compounds, Ligands, Metal Ions, Peptides, Scaffolds (biology), Ferric Ion, Hemoprotein, Metalloprotein, Amino Acid Sequence, Article, Binding Site, Catalysis, Chemical Model, Circular Dichroism, Kinetics, Metabolism, Oxidation Reduction Reaction, Protein Engineering, Protein Secondary Structure, Synthesis, Ultraviolet Spectrophotometry, Ferric Compounds, Hemeproteins, Oxidation-Reduction, Protein Structure,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, Complesso Universitario Monte S. Angelo, University of Naples Federico II, Via Cintia, 80126 Naples, Italy
Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, Netherlands
IBB, CNR, Via Mezzocannone 16, 80134 Napoli, Italy
References:
Montellano, P.R.O.D., (2004) Cytochrome P450: Structure, Mechanism, and Biochemistry, p. 689. , 3 rd ed., Kluwer Academic/Plenum Publishers, New York,
Meunier, B., De Visser, S.P., Shaik, S., (2004) Chem. Rev., 104, pp. 3947-3980
Morris, D.L., Hager, L.P., (1966) J. Biol. Chem., 241, pp. 1763-1768
Sundaramoorthy, M., Terner, J., Poulos, T.L., (1995) Structure, 3, pp. 1367-1377
Perutz, M.F., Muirhead, H., Cox, J.M., Goaman, L.C.G., Mathews, F.S., McGandy, E.L., Webb, L.E., (1968) Nature, 219, pp. 29-32
Shikama, K., (1998) Chem. Rev., 98, pp. 1357-1373
Van Deurzen, M.P.J.V., Rantwijk, F.V., Sheldon, R.A., (1997) Tetrahedron, 53, pp. 13183-13220
Veitch, N.C., (2004) Phytochemistry, 65, pp. 249-259
Lu, Y., Yeung, N., Sieracki, N., Marshall, N.M., (2009) Nature, 460, pp. 855-862
Nanda, V., Koder, R.L., (2010) Nat. Chem., 2, pp. 15-24
Smith, B.A., Hecht, M.H., (2011) Curr. Opin. Chem. Biol., 15, pp. 421-426
Kamtekar, S., Schiffer, J.M., Xiong, H., Babik, J.M., Hecht, M.H., (1993) Science, 262, pp. 1680-1685
Koder, R.L., Anderson, J.L., Solomon, L.A., Reddy, K.S., Moser, C.C., Dutton, P.L., (2009) Nature, 458, pp. 305-309
Ghirlanda, G., Osyczka, A., Liu, W., Antolovich, M., Smith, K.M., Dutton, P.L., Wand, A.J., Degrado, W.F., (2004) J. Am. Chem. Soc., 126, pp. 8141-8147
Gibney, B.R., Huang, S.S., Skalicky, J.J., Fuentes, E.J., Wand, A.J., Dutton, P.L., (2001) Biochemistry, 40, pp. 10550-10561
Benson, D.R., Hart, B.R., Zhu, X., Doughty, M.B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Robertson, D.E., Farid, R.S., Moser, C.C., Urbauer, J.L., Mulholland, S.E., Pidikiti, R., Lear, J.D., Dutton, P.L., (1994) Nature, 368, pp. 425-432
Ishida, M., Dohmae, N., Shiro, Y., Oku, T., Iizuka, T., Isogai, Y., (2004) Biochemistry, 43, pp. 9823-9833
Monien, B.H., Drepper, F., Sommerhalter, M., Lubitz, W., Haehnel, W., (2007) J. Mol. Biol., 371, pp. 739-753
Nastri, F., Lista, L., Ringhieri, P., Vitale, R., Faiella, M., Andreozzi, C., Travascio, P., Pavone, V., (2011) Chem. Eur. J., 17, pp. 4444-4453
Zhuang, J., Amoroso, J.H., Kinloch, R., Dawson, J.H., Baldwin, M.J., Gibney, B.R., (2004) Inorg. Chem., 43, pp. 8218-8220
Wei, Y., Kim, S., Fela, D., Baum, J., Hecht, M.H., (2003) Proc. Natl. Acad. Sci. USA, 100, pp. 13270-13273
Wei, Y., Liu, T., Sazinsky, S.L., Moffet, D.A., Pelczer, I., Hecht, M.H., (2003) Protein Sci., 12, pp. 92-102
Moffet, D.A., Case, M.A., House, J.C., Vogel, K., Williams, R.D., Spiro, T.G., McLendon, G.L., Hecht, M.H., (2001) J. Am. Chem. Soc., 123, pp. 2109-2115
Das, A., Hecht, M.H., (2007) J. Inorg. Biochem., 101, pp. 1820-1826
Frolow, F., Kalb, A.J., Yariv, J., (1994) Nat. Struct. Biol., 1, pp. 453-460
Aurora, R., Srinivasan, R., Rose, G.D., (1994) Science, 264, pp. 1126-1130
Lahr, S.J., Engel, D.E., Stayrook, S.E., Maglio, O., North, B., Geremia, S., Lombardi, A., Degrado, W.F., (2005) J. Mol. Biol., 346, pp. 1441-1454
Aurora, R., Rose, G.D., (1998) Protein Sci., 7, pp. 21-38
Richardson, J.S., Richardson, D.C., (1988) Science, 240, pp. 1648-1652
Doig, A.J., Baldwin, R.L., (1995) Protein Sci., 4, pp. 1325-1335
Buchler, J.W., (1979) The Porphyrins, Vol. 1, Structure and Synthesis, Part A, pp. 389-483. , in (Ed.: D. Dolphin), Academic Press, New York
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
Greenfield, N.J., Fasman, G.D., (1969) Biochemistry, 8, pp. 4108-4116
Perez-Iratxeta, C., Andrade-Navarro, M.A., (2008) BMC Struct. Biol., 8, pp. 25-29
Makinen, M.W., Churg, A.K., (1983) Physical Bioinorganic Chemistry, Vol. 1, Iron Porphyrins, Part i, pp. 141-235. , in (Eds.: A. B. P. Lever, H. B. Gray), Addison-Wesley, Reading
Feis, A., Marzocchi, M.P., Paoli, M., Smulevich, G., (1994) Biochemistry, 33, pp. 4577-4583
Kennedy, M.L., Silchenko, S., Houndonougbo, N., Gibney, B.R., Dutton, P.L., Rodgers, K.R., Benson, D.R., (2001) J. Am. Chem. Soc., 123, pp. 4635-4636
Blumberg, W.E., Peisach, J., Wittenberg, B.A., Wittenberg, J.B., (1968) J. Biol. Chem., 243, pp. 1854-1862
Vickery, L., Nozawa, T., Sauer, K., (1976) J. Am. Chem. Soc., 98, pp. 343-350
Kobayashi, N., Tsunenori, N., Hatano, M., (1977) Biochim. Biophys. Acta Protein Struct., 493, pp. 340-351
Nozawa, T., Kobayashi, N., Hatano, M., (1976) Biochim. Biophys. Acta Protein Struct., 427, pp. 652-662
Degrado, W.F., Summa, C.M., Pavone, V., Nastri, F., Lombardi, A., (1999) Annu. Rev. Biochem., 68, pp. 779-819
Wang, J., Araki, T., Matsuoka, M., Ogawa, T., (1999) Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1435, pp. 177-183
Sakamoto, S., Sakurai, S., Ueno, A., Mihara, H., (1997) Chem. Commun., pp. 1221-1222
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., Montellano, P.R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Mahy, J.-P., Raffy, Q., Allard, M., Ricoux, R., (2009) Biochimie, 91, pp. 1321-1323
Ricoux, R., Raffy, Q., Mahy, J.-P., (2007) C. R. Chim., 10, pp. 684-702
De Lauzon, S., Mansuy, D., Mahy, J.-P., (2002) Eur. J. Biochem., 269, pp. 470-480
Romesberg, F.E., Santarsiero, B.D., Spiller, B., Yin, J., Barnes, D., Schultz, P.G., Stevens, R.C., (1998) Biochemistry, 37, pp. 14404-14409
De Lauzon, S., Quilez, R., Lion, L., Desfosses, B., Desfosses, B., Lee, I., Sari, M.-A., Mahy, J.-P., (1998) Eur. J. Biochem., 257, pp. 121-130
De Lauzon, S., Desfosses, B., Mansuy, D., Mahy, J.-P., (1999) FEBS Lett., 443, pp. 229-234
Kunishima, N., Amada, F., Fukuyama, K., Kawamoto, M., Matsunaga, T., Matsubara, H., (1996) FEBS Lett., 378, pp. 291-294
Pond, A.E., Sono, M., Elenkova, E.A., McRee, D.E., Goodin, D.B., English, A.M., Dawson, J.H., (1999) J. Inorg. Biochem., 76, pp. 165-174
Suzuki, S., (1991) J. Inorg. Biochem., 44, pp. 267-276
Howes, B.D., Rodriguez-Lopez, J.N., Smith, A.T., Smulevich, G., (1997) Biochemistry, 36, pp. 1532-1543
Marques, H.M., (2007) Dalton Trans., pp. 4371-4385
Matthew, J.B., (1985) Ann. Rev. Biophys. Biophys. Chem., 14, pp. 387-417
Dawson, J.H., Dooley, D.M., (1989) Physical Bioinorganic Chemistry, Vol. 4, Iron Porphyrins, Part III, pp. 1-136. , in (Eds.: A. B. P. Lever, H. B. Gray), VCH, New York
Neri, F., Kok, D., Miller, M.A., Smulevich, G., (1997) Biochemistry, 36, pp. 8947-8953
Asakura, T., Reed, G.H., Leigh, J.S., (1972) Biochemistry, 11, pp. 334-338
Dunford, H.B., Stillman, J.S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Poulos, T.L., Kraut, J., (1980) J. Biol. Chem., 255, pp. 8199-8205
Erman, J.E., Vitello, L.B., Miller, M.A., Shaw, A., Brown, K.A., Kraut, J., (1993) Biochemistry, 32, pp. 9798-9806
Newmyer, S.L., De Montellano, P.R.O., (1995) J. Biol. Chem., 270, pp. 19430-19438
Rodríguez-López, J.N., Lowe, D.J., Hernández-Ruiz, J., Hiner, A.N.P., García-Cánovas, F., Thorneley, R.N.F., (2001) J. Am. Chem. Soc., 123, pp. 11838-11847
Vitello, L.B., Erman, J.E., Miller, M.A., Wang, J., Kraut, J., (1993) Biochemistry, 32, pp. 9807-9818
Dawson, J.H., Sono, M., (1987) Chem. Rev., 87, pp. 1255-1276
Dolphin, D., Forman, A., Borg, D.C., Fajer, J., Felton, R.H., (1971) Proc. Natl. Acad. Sci. USA, 68, pp. 614-618
Schonbaum, G.R., Lo, S., (1972) J. Biol. Chem., 247, pp. 3353-3360
Dunford, H.B., (1991) Peroxidases in Chemistry and Biology, Vol. 2, pp. 1-24. , in (Eds.: J. Everse, K. E. Everse, M. B. Grisham), CRC Press, Boca Raton
Egawa, T., Shimada, H., Ishimura, Y., (2000) J. Biol. Chem., 275, pp. 34858-34866
Matsui, T., Ozaki S.-I, Liong, E., Phillips, G.N., Watanabe, Y., (1999) J. Biol. Chem., 274, pp. 2838-2844
Fox, J.B., Nicholas, R.A., Ackerman, S.A., Swift, C.E., (1974) Biochemistry, 13, pp. 5178-5186
English, A.M., Tsaprailis, G., (1995) Adv. Inorg. Chem., 43, pp. 79-125
Allentoff, A.J., Bolton, J.L., Wilks, A., Thompson, J.A., Ortiz De Montellano, P.R., (1992) J. Am. Chem. Soc., 114, pp. 9744-9749
Barlow, S., Rohl, A.L., Shi, S., Freeman, C.M., O'Hare, D., (1996) J. Am. Chem. Soc., 118, pp. 7578-7592
Childs, B.R.E., Bardsley, W.G., (1975) Biochem. J., 145, pp. 93-103
Cleland, W.W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
Takakuwa, T., Konno, T., Meguro, H., (1985) Anal. Sci., 1, pp. 215-218
Holmquist, B., (1986) Methods Enzymol., 130, pp. 270-290
Montellano, P. R. O. D., (2004) Cytochrome P450: Structure, Mechanism, and Biochemistry, p. 689. , 3 rd ed., Kluwer Academic/Plenum Publishers, New York,
Morris, D. L., Hager, L. P., (1966) J. Biol. Chem., 241, pp. 1763-1768
Perutz, M. F., Muirhead, H., Cox, J. M., Goaman, L. C. G., Mathews, F. S., McGandy, E. L., Webb, L. E., (1968) Nature, 219, pp. 29-32
Van Deurzen, M. P. J. V., Rantwijk, F. V., Sheldon, R. A., (1997) Tetrahedron, 53, pp. 13183-13220
Veitch, N. C., (2004) Phytochemistry, 65, pp. 249-259
Smith, B. A., Hecht, M. H., (2011) Curr. Opin. Chem. Biol., 15, pp. 421-426
Koder, R. L., Anderson, J. L., Solomon, L. A., Reddy, K. S., Moser, C. C., Dutton, P. L., (2009) Nature, 458, pp. 305-309
Gibney, B. R., Huang, S. S., Skalicky, J. J., Fuentes, E. J., Wand, A. J., Dutton, P. L., (2001) Biochemistry, 40, pp. 10550-10561
Benson, D. R., Hart, B. R., Zhu, X., Doughty, M. B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Robertson, D. E., Farid, R. S., Moser, C. C., Urbauer, J. L., Mulholland, S. E., Pidikiti, R., Lear, J. D., Dutton, P. L., (1994) Nature, 368, pp. 425-432
Monien, B. H., Drepper, F., Sommerhalter, M., Lubitz, W., Haehnel, W., (2007) J. Mol. Biol., 371, pp. 739-753
Moffet, D. A., Case, M. A., House, J. C., Vogel, K., Williams, R. D., Spiro, T. G., McLendon, G. L., Hecht, M. H., (2001) J. Am. Chem. Soc., 123, pp. 2109-2115
Das, A., Hecht, M. H., (2007) J. Inorg. Biochem., 101, pp. 1820-1826
Lahr, S. J., Engel, D. E., Stayrook, S. E., Maglio, O., North, B., Geremia, S., Lombardi, A., Degrado, W. F., (2005) J. Mol. Biol., 346, pp. 1441-1454
Richardson, J. S., Richardson, D. C., (1988) Science, 240, pp. 1648-1652
Doig, A. J., Baldwin, R. L., (1995) Protein Sci., 4, pp. 1325-1335
Buchler, J. W., (1979) The Porphyrins, Vol. 1, Structure and Synthesis, Part A, pp. 389-483. , in (Ed.: D. Dolphin), Academic Press, New York
Greenfield, N. J., Fasman, G. D., (1969) Biochemistry, 8, pp. 4108-4116
Makinen, M. W., Churg, A. K., (1983) Physical Bioinorganic Chemistry, Vol. 1, Iron Porphyrins, Part i, pp. 141-235. , in (Eds.: A. B. P. Lever, H. B. Gray), Addison-Wesley, Reading
Kennedy, M. L., Silchenko, S., Houndonougbo, N., Gibney, B. R., Dutton, P. L., Rodgers, K. R., Benson, D. R., (2001) J. Am. Chem. Soc., 123, pp. 4635-4636
Blumberg, W. E., Peisach, J., Wittenberg, B. A., Wittenberg, J. B., (1968) J. Biol. Chem., 243, pp. 1854-1862
Degrado, W. F., Summa, C. M., Pavone, V., Nastri, F., Lombardi, A., (1999) Annu. Rev. Biochem., 68, pp. 779-819
Savenkova, M. I., Kuo, J. M., Ortiz De Montellano, P. R., (1998) Biochemistry, 37, pp. 10828-10836
Savenkova, M. I., Newmyer, S. L., Montellano, P. R., (1996) J. Biol. Chem., 271, pp. 24598-24603
Mahy, J. -P., Raffy, Q., Allard, M., Ricoux, R., (2009) Biochimie, 91, pp. 1321-1323
Romesberg, F. E., Santarsiero, B. D., Spiller, B., Yin, J., Barnes, D., Schultz, P. G., Stevens, R. C., (1998) Biochemistry, 37, pp. 14404-14409
Pond, A. E., Sono, M., Elenkova, E. A., McRee, D. E., Goodin, D. B., English, A. M., Dawson, J. H., (1999) J. Inorg. Biochem., 76, pp. 165-174
Howes, B. D., Rodriguez-Lopez, J. N., Smith, A. T., Smulevich, G., (1997) Biochemistry, 36, pp. 1532-1543
Marques, H. M., (2007) Dalton Trans., pp. 4371-4385
Matthew, J. B., (1985) Ann. Rev. Biophys. Biophys. Chem., 14, pp. 387-417
Dawson, J. H., Dooley, D. M., (1989) Physical Bioinorganic Chemistry, Vol. 4, Iron Porphyrins, Part III, pp. 1-136. , in (Eds.: A. B. P. Lever, H. B. Gray), VCH, New York
Dunford, H. B., Stillman, J. S., (1976) Coord. Chem. Rev., 19, pp. 187-251
Poulos, T. L., Kraut, J., (1980) J. Biol. Chem., 255, pp. 8199-8205
Erman, J. E., Vitello, L. B., Miller, M. A., Shaw, A., Brown, K. A., Kraut, J., (1993) Biochemistry, 32, pp. 9798-9806
Newmyer, S. L., De Montellano, P. R. O., (1995) J. Biol. Chem., 270, pp. 19430-19438
Rodr guez-L pez, J. N., Lowe, D. J., Hern ndez-Ruiz, J., Hiner, A. N. P., Garc a-C novas, F., Thorneley, R. N. F., (2001) J. Am. Chem. Soc., 123, pp. 11838-11847
Vitello, L. B., Erman, J. E., Miller, M. A., Wang, J., Kraut, J., (1993) Biochemistry, 32, pp. 9807-9818
Dawson, J. H., Sono, M., (1987) Chem. Rev., 87, pp. 1255-1276
Schonbaum, G. R., Lo, S., (1972) J. Biol. Chem., 247, pp. 3353-3360
Dunford, H. B., (1991) Peroxidases in Chemistry and Biology, Vol. 2, pp. 1-24. , in (Eds.: J. Everse, K. E. Everse, M. B. Grisham), CRC Press, Boca Raton
Fox, J. B., Nicholas, R. A., Ackerman, S. A., Swift, C. E., (1974) Biochemistry, 13, pp. 5178-5186
English, A. M., Tsaprailis, G., (1995) Adv. Inorg. Chem., 43, pp. 79-125
Allentoff, A. J., Bolton, J. L., Wilks, A., Thompson, J. A., Ortiz De Montellano, P. R., (1992) J. Am. Chem. Soc., 114, pp. 9744-9749
Childs, B. R. E., Bardsley, W. G., (1975) Biochem. J., 145, pp. 93-103
Cleland, W. W., (1963) Biochim. Biophys. Acta, 67, pp. 104-137
De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein
A new artificial metalloenzyme, MP3 (MiniPeroxidase 3), designed by combining the excellent structural properties of four-helix bundle protein scaffolds with the activity of natural peroxidases, was synthesised and characterised. This new hemeprotein model was developed by covalently linking the deuteroporphyrin to two peptide chains of different compositions to obtain an asymmetric helixloophelix/heme/helixloophelix sandwich arrangement, characterised by 1) a His residue on one chain that acts as an axial ligand to the iron ion; 2) a vacant distal site that is able to accommodate exogenous ligands or substrates; and 3) an Arg residue in the distal site that should assist in hydrogen peroxide activation to give an HRP-like catalytic process. MP3 was synthesised and characterised as its iron complex. CD measurements revealed the high helix-forming propensity of the peptide, confirming the appropriateness of the model procedure; UV/Vis, MCD and EPR experiments gave insights into the coordination geometry and the spin state of the metal. Kinetic experiments showed that FeIIIMP3 possesses peroxidase-like activity comparable to R38AhHRP, highlighting the possibility of mimicking the functional features of natural enzymes. The synergistic application of de novo design methods, synthetic procedures, and spectroscopic characterisation, described herein, demonstrates a method by which to implement and optimise catalytic activity for an enzyme mimetic.
A new artificial metalloenzyme, MP3 (MiniPeroxidase 3), designed by combining the excellent structural properties of four-helix bundle protein scaffolds with the activity of natural peroxidases, was synthesised and characterised. This new hemeprotein model was developed by covalently linking the deuteroporphyrin to two peptide chains of different compositions to obtain an asymmetric helixloophelix/heme/helixloophelix sandwich arrangement, characterised by 1) a His residue on one chain that acts as an axial ligand to the iron ion; 2) a vacant distal site that is able to accommodate exogenous ligands or substrates; and 3) an Arg residue in the distal site that should assist in hydrogen peroxide activation to give an HRP-like catalytic process. MP3 was synthesised and characterised as its iron complex. CD measurements revealed the high helix-forming propensity of the peptide, confirming the appropriateness of the model procedure; UV/Vis, MCD and EPR experiments gave insights into the coordination geometry and the spin state of the metal. Kinetic experiments showed that FeIIIMP3 possesses peroxidase-like activity comparable to R38AhHRP, highlighting the possibility of mimicking the functional features of natural enzymes. The synergistic application of de novo design methods, synthetic procedures, and spectroscopic characterisation, described herein, demonstrates a method by which to implement and optimise catalytic activity for an enzyme mimetic.
De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein
| ▼ Syntethic metalloproteins and peptides for biosensing applications |
De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein
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 (241 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 (451 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 315: 67-89.
Impact Factor: 13.324
View Export to BibTeX Export to EndNote
Chino M, Leone L, Maglio O, Lombardi A
* Designing Covalently Linked Heterodimeric Four-Helix Bundles (294 views) (PDF 179 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic), 2016; 580: 471-499.
Impact Factor: 1.972
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
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
Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
* 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.
Impact Factor: 5.925
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 (481 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 (927 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
* 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 (241 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 (451 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 315: 67-89.
Impact Factor: 13.324
View Export to BibTeX Export to EndNote
Chino M, Leone L, Maglio O, Lombardi A
* Designing Covalently Linked Heterodimeric Four-Helix Bundles (294 views) (PDF 179 views)
Method Enzymol (ISSN: 0076-6879, 1557-7988electronic), 2016; 580: 471-499.
Impact Factor: 1.972
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
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
Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
* 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.
Impact Factor: 5.925
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 (481 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 (927 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
17 Records (17 excluding Abstracts).
Total impact factor: 91.606 (91.606 excluding Abstracts).
Total 5 year impact factor: 87.581 (87.581 excluding Abstracts).
Total impact factor: 91.606 (91.606 excluding Abstracts).
Total 5 year impact factor: 87.581 (87.581 excluding Abstracts).
474 views. Last view on Monday 16 January 2023, 9:06:44
ibb.cnr.it
