An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization (415 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
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Paper type: Journal Article,
Impact factor: 3.559, 5-year impact factor: 3.367
Url: http://pubs.rsc.org/en/content/articlepdf/2015/ob/c5ob00257e
Keywords: Magnetic Circular-Dichroism, De-Novo Design, Horseradish-Peroxidase, Helix Sandwich, Cytochrome-C, Miniaturized Hemoproteins, Molecular-Dynamics, Aqueous-Solution, Mimochrome Vi, Peptide, Amino Acids, Enzyme Activity, Porphyrins, Rational Functions, Scaffolds, Scaffolds (biology), Amino Acid Substitution, Artificial Heme Enzymes, Asymmetric System, Enhanced Catalytic Activity, Functional Screening, Peroxidase Activities, Peroxidase-Like Activities, Structural Characterization, Catalyst Activity,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples, "Federico II", Via Cintia, 80126 Naples, Italy.
Collège de France, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France
IBB, CNR, Via Mezzocannone 16, 80134 Naples, Italy
IMAST Scarl, Piazza Bovio 22, 80133 Naples, Italy
References:
Maglio, O., Nastri, F., Lombardi, A., (2012) Ionic Interactions in Natural and Synthetic Macromolecules, pp. 361-450. , ed. A. Ciferri and A. Perico, John Wiley & Sons, Inc., Hoboken, NJ, US
Sontz, P.A., Song, W.J., Tezcan, F.A., (2014) Curr. Opin. Chem. Biol., 19, pp. 42-49
Nastri, F., Bruni, R., Maglio, O., Lombardi, A., (2013) Coordination Chemistry in Protein Cages, pp. 43-85. , ed. T. Ueno and Y. Watanabe, John Wiley & Sons, Inc
Reig, A.J., Pires, M.M., Snyder, R.A., Wu, Y., Jo, H., Kulp, D.W., Butch, S.E., Degrado, W.F., (2012) Nat. Chem., 4, pp. 900-906
Zastrow, M.L., Peacock, A.F.A., Stuckey, J.A., Pecoraro, V.L., (2011) Nat. Chem., 4, pp. 118-123
Yu, F., Cangelosi, V.M., Zastrow, M.L., Tegoni, M., Plegaria, J.S., Tebo, A.G., Mocny, C.S., Pecoraro, V.L., (2014) Chem. Rev., , 140324100753004
Kaplan, J., Degrado, W.F., (2004) Proc. Natl. Acad. Sci. U. S. A., 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
Torres Martin De Rosales, R., Faiella, M., Farquhar, E., Que, L., Andreozzi, C., Pavone, V., Maglio, O., Lombardi, A., (2010) JBIC, J. Biol. Inorg. Chem., 15, pp. 717-728
Nastri, F., Lista, L., Ringhieri, P., Vitale, R., Faiella, M., Andreozzi, C., Travascio, P., Pavone, V., (2011) Chem. - Eur. J., 17, pp. 4444-4453
Faiella, M., Maglio, O., Nastri, F., Lombardi, A., Lista, L., Hagen, W.R., Pavone, V., (2012) Chem. - Eur. J., 18, pp. 15960-15971
Koder, R.L., Anderson, J.L.R., Solomon, L.A., Reddy, K.S., Moser, C.C., Dutton, P.L., (2009) Nature, 458, pp. 305-309
Petrik, I.D., Liu, J., Lu, Y., (2014) Curr. Opin. Chem. Biol., 19, pp. 67-75
Dürrenberger, M., Ward, T.R., (2014) Curr. Opin. Chem. Biol., 19, pp. 99-106
Anderson, J.L.R., Armstrong, C.T., Kodali, G., Lichtenstein, B.R., Watkins, D.W., Mancini, J.A., Boyle, A.L., Dutton, P.L., (2014) Chem. Sci., 5, p. 507
Lombardi, A., Nastri, F., Pavone, V., (2001) Chem. Rev., 101, pp. 3165-3190
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
Costanzo, L., Geremia, S., Randaccio, L., Nastri, F., Maglio, O., Lombardi, A., Pavone, V., (2004) JBIC, J. Biol. Inorg. Chem., 9, pp. 1017-1027
Vicari, C., Saraiva, I.H., Maglio, O., Nastri, F., Pavone, V., Louro, R.O., Lombardi, A., (2014) Chem. Commun., 50, p. 3852
Ranieri, A., Monari, S., Sola, M., Borsari, M., Battistuzzi, G., Ringhieri, P., Nastri, F., Lombardi, A., (2010) Langmuir, 26, pp. 17831-17835
Vitale, R., Lista, L., Lau-Truong, S., Tucker, R.T., Brett, M.J., Limoges, B., Pavone, V., Balland, V., (2014) Chem. Commun., 50, p. 1894
Humphrey, W., Dalke, A., Schulten, K., (1996) J. Mol. Graphics, 14, pp. 33-38
O'Neil, K., Degrado, W., (1990) Science, 250, pp. 646-651
Buchler, J.W., (1979) The Porphyrins, 1, pp. 389-483. , Academic Press, NY, USA
Rodriguez-Lopez, J.N., Smith, A.T., Thorneley, R.N., (1996) J. Biol. Chem., 271, pp. 4023-4030
Marques, H.M., (2007) Dalton Trans, pp. 4371-4385
Vickery, L., Nozawa, T., Sauer, K., (1976) J. Am. Chem. Soc., 98, pp. 351-357
Hatano, M., Nozawa, T., (1978) Adv. Biophys., 11, pp. 95-149
Nozawa, T., Kobayashi, N., Hatano, M., (1976) Biochim. Biophys. Acta, 427, pp. 652-662
Kobayashi, N., Nozawa, T., Hatano, M., (1977) Biochim. Biophys. Acta, 493, pp. 340-351
Nagai, M., Nagai, Y., Imai, K., Neya, S., (2014) Chirality, 26, pp. 438-442
Blauer, G., Sreerama, N., Woody, R.W., (1993) Biochemistry, 32, pp. 6674-6679
Kajiyoshi, M., Anan, F.K., (1975) J. Biochem., 78, pp. 1087-1095
Blanco, F.J., Rivas, G., Serrano, L., (1994) Nat. Struct. Biol., 1, pp. 584-590
Jasanoff, A., Fersht, A.R., (1994) Biochemistry, 33, pp. 2129-2135
Main, E.R., Jackson, S.E., (1999) Nat. Struct. Biol., 6, pp. 831-835
Hong, D.-P., Hoshino, M., Kuboi, R., Goto, Y., (1999) J. Am. Chem. Soc., 121, pp. 8427-8433
Reiersen, H., Rees, A.R., (2000) Protein Eng., Des. Sel., 13, pp. 739-743
Roccatano, D., Colombo, G., Fioroni, M., Mark, A.E., (2002) Proc. Natl. Acad. Sci. U. S. A., 99, pp. 12179-12184
Poulos, T.L., Kraut, J., (1980) J. Biol. Chem., 255, pp. 8199-8205
Azevedo, A.M., Martins, V.C., Prazeres, D.M.F., Vojinović, V., Cabral, J.M.S., Fonseca, L.P., (2003) Biotechnology Annual Review, 9, pp. 199-247. , Elsevier
Veitch, N.C., (2004) Phytochemistry, 65, pp. 249-259
Newmyer, S.L., De Montellano, P.R., (1996) J. Biol. Chem., 271, pp. 14891-14896
Savenkova, M.I., Kuo, J.M., Ortiz De Montellano, P.R., (1998) Biochemistry, 37, pp. 10828-10836
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2015 Apr 22; 13(17): 4859-4868.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.559, 5-year impact factor: 3.367
Url: http://pubs.rsc.org/en/content/articlepdf/2015/ob/c5ob00257e
Keywords: Magnetic Circular-Dichroism, De-Novo Design, Horseradish-Peroxidase, Helix Sandwich, Cytochrome-C, Miniaturized Hemoproteins, Molecular-Dynamics, Aqueous-Solution, Mimochrome Vi, Peptide, Amino Acids, Enzyme Activity, Porphyrins, Rational Functions, Scaffolds, Scaffolds (biology), Amino Acid Substitution, Artificial Heme Enzymes, Asymmetric System, Enhanced Catalytic Activity, Functional Screening, Peroxidase Activities, Peroxidase-Like Activities, Structural Characterization, Catalyst Activity,
Affiliations:
*** IBB - CNR ***
Department of Chemical Sciences, University of Naples, "Federico II", Via Cintia, 80126 Naples, Italy.
Collège de France, 11 place Marcelin Berthelot, 75231 Paris Cedex 05, France
IBB, CNR, Via Mezzocannone 16, 80134 Naples, Italy
IMAST Scarl, Piazza Bovio 22, 80133 Naples, Italy
References:
Maglio, O., Nastri, F., Lombardi, A., (2012) Ionic Interactions in Natural and Synthetic Macromolecules, pp. 361-450. , ed. A. Ciferri and A. Perico, John Wiley & Sons, Inc., Hoboken, NJ, US
Sontz, P.A., Song, W.J., Tezcan, F.A., (2014) Curr. Opin. Chem. Biol., 19, pp. 42-49
Nastri, F., Bruni, R., Maglio, O., Lombardi, A., (2013) Coordination Chemistry in Protein Cages, pp. 43-85. , ed. T. Ueno and Y. Watanabe, John Wiley & Sons, Inc
Reig, A.J., Pires, M.M., Snyder, R.A., Wu, Y., Jo, H., Kulp, D.W., Butch, S.E., Degrado, W.F., (2012) Nat. Chem., 4, pp. 900-906
Zastrow, M.L., Peacock, A.F.A., Stuckey, J.A., Pecoraro, V.L., (2011) Nat. Chem., 4, pp. 118-123
Yu, F., Cangelosi, V.M., Zastrow, M.L., Tegoni, M., Plegaria, J.S., Tebo, A.G., Mocny, C.S., Pecoraro, V.L., (2014) Chem. Rev., , 140324100753004
Kaplan, J., Degrado, W.F., (2004) Proc. Natl. Acad. Sci. U. S. A., 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
Torres Martin De Rosales, R., Faiella, M., Farquhar, E., Que, L., Andreozzi, C., Pavone, V., Maglio, O., Lombardi, A., (2010) JBIC, J. Biol. Inorg. Chem., 15, pp. 717-728
Nastri, F., Lista, L., Ringhieri, P., Vitale, R., Faiella, M., Andreozzi, C., Travascio, P., Pavone, V., (2011) Chem. - Eur. J., 17, pp. 4444-4453
Faiella, M., Maglio, O., Nastri, F., Lombardi, A., Lista, L., Hagen, W.R., Pavone, V., (2012) Chem. - Eur. J., 18, pp. 15960-15971
Koder, R.L., Anderson, J.L.R., Solomon, L.A., Reddy, K.S., Moser, C.C., Dutton, P.L., (2009) Nature, 458, pp. 305-309
Petrik, I.D., Liu, J., Lu, Y., (2014) Curr. Opin. Chem. Biol., 19, pp. 67-75
Dürrenberger, M., Ward, T.R., (2014) Curr. Opin. Chem. Biol., 19, pp. 99-106
Anderson, J.L.R., Armstrong, C.T., Kodali, G., Lichtenstein, B.R., Watkins, D.W., Mancini, J.A., Boyle, A.L., Dutton, P.L., (2014) Chem. Sci., 5, p. 507
Lombardi, A., Nastri, F., Pavone, V., (2001) Chem. Rev., 101, pp. 3165-3190
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
Costanzo, L., Geremia, S., Randaccio, L., Nastri, F., Maglio, O., Lombardi, A., Pavone, V., (2004) JBIC, J. Biol. Inorg. Chem., 9, pp. 1017-1027
Vicari, C., Saraiva, I.H., Maglio, O., Nastri, F., Pavone, V., Louro, R.O., Lombardi, A., (2014) Chem. Commun., 50, p. 3852
Ranieri, A., Monari, S., Sola, M., Borsari, M., Battistuzzi, G., Ringhieri, P., Nastri, F., Lombardi, A., (2010) Langmuir, 26, pp. 17831-17835
Vitale, R., Lista, L., Lau-Truong, S., Tucker, R.T., Brett, M.J., Limoges, B., Pavone, V., Balland, V., (2014) Chem. Commun., 50, p. 1894
Humphrey, W., Dalke, A., Schulten, K., (1996) J. Mol. Graphics, 14, pp. 33-38
O'Neil, K., Degrado, W., (1990) Science, 250, pp. 646-651
Buchler, J.W., (1979) The Porphyrins, 1, pp. 389-483. , Academic Press, NY, USA
Rodriguez-Lopez, J.N., Smith, A.T., Thorneley, R.N., (1996) J. Biol. Chem., 271, pp. 4023-4030
Marques, H.M., (2007) Dalton Trans, pp. 4371-4385
Vickery, L., Nozawa, T., Sauer, K., (1976) J. Am. Chem. Soc., 98, pp. 351-357
Hatano, M., Nozawa, T., (1978) Adv. Biophys., 11, pp. 95-149
Nozawa, T., Kobayashi, N., Hatano, M., (1976) Biochim. Biophys. Acta, 427, pp. 652-662
Kobayashi, N., Nozawa, T., Hatano, M., (1977) Biochim. Biophys. Acta, 493, pp. 340-351
Nagai, M., Nagai, Y., Imai, K., Neya, S., (2014) Chirality, 26, pp. 438-442
Blauer, G., Sreerama, N., Woody, R.W., (1993) Biochemistry, 32, pp. 6674-6679
Kajiyoshi, M., Anan, F.K., (1975) J. Biochem., 78, pp. 1087-1095
Blanco, F.J., Rivas, G., Serrano, L., (1994) Nat. Struct. Biol., 1, pp. 584-590
Jasanoff, A., Fersht, A.R., (1994) Biochemistry, 33, pp. 2129-2135
Main, E.R., Jackson, S.E., (1999) Nat. Struct. Biol., 6, pp. 831-835
Hong, D.-P., Hoshino, M., Kuboi, R., Goto, Y., (1999) J. Am. Chem. Soc., 121, pp. 8427-8433
Reiersen, H., Rees, A.R., (2000) Protein Eng., Des. Sel., 13, pp. 739-743
Roccatano, D., Colombo, G., Fioroni, M., Mark, A.E., (2002) Proc. Natl. Acad. Sci. U. S. A., 99, pp. 12179-12184
Poulos, T.L., Kraut, J., (1980) J. Biol. Chem., 255, pp. 8199-8205
Azevedo, A.M., Martins, V.C., Prazeres, D.M.F., Vojinović, V., Cabral, J.M.S., Fonseca, L.P., (2003) Biotechnology Annual Review, 9, pp. 199-247. , Elsevier
Veitch, N.C., (2004) Phytochemistry, 65, pp. 249-259
Newmyer, S.L., De Montellano, P.R., (1996) J. Biol. Chem., 271, pp. 14891-14896
Savenkova, M.I., Kuo, J.M., Ortiz De Montellano, P.R., (1998) Biochemistry, 37, pp. 10828-10836
An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization
Synthetic proteins represent useful tools for reproducing metalloprotein functions in minimal, well-defined scaffolds. Herein, we describe the rational refinement of function into heme-protein models from the Mimochrome family. Originally designed to mimic the bis-His cytochrome b, the Mimochrome structure was modified to introduce a peroxidase-like activity, by creating a distal cavity on the heme. The success with the first asymmetric system, Mimochrome VI (MC6), gave the opportunity to explore further modifications in order to improve the catalytic activity. Starting from ferric MC6, single amino acid substitutions were introduced in the peptide chains to obtain four compounds, which were screened for peroxidase activity. The detailed structural and functional analysis of the best analogue, FeIII-E2L(TD)-MC6, indicates that an arginine residue in proximity to the heme-distal site could assist with catalysis by favoring the formation of the intermediate "compound I", thus mimicking R38 in HRP. This result highlights the potential of using small scaffolds for exploring the main factors that tune the heme-protein activity, and for programming new desired functions. This journal is © The Royal Society of Chemistry 2015.
Synthetic proteins represent useful tools for reproducing metalloprotein functions in minimal, well-defined scaffolds. Herein, we describe the rational refinement of function into heme-protein models from the Mimochrome family. Originally designed to mimic the bis-His cytochrome b, the Mimochrome structure was modified to introduce a peroxidase-like activity, by creating a distal cavity on the heme. The success with the first asymmetric system, Mimochrome VI (MC6), gave the opportunity to explore further modifications in order to improve the catalytic activity. Starting from ferric MC6, single amino acid substitutions were introduced in the peptide chains to obtain four compounds, which were screened for peroxidase activity. The detailed structural and functional analysis of the best analogue, FeIII-E2L(TD)-MC6, indicates that an arginine residue in proximity to the heme-distal site could assist with catalysis by favoring the formation of the intermediate "compound I", thus mimicking R38 in HRP. This result highlights the potential of using small scaffolds for exploring the main factors that tune the heme-protein activity, and for programming new desired functions. This journal is © The Royal Society of Chemistry 2015.
An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization
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An artificial heme-enzyme with enhanced catalytic activity: evolution, functional screening and structural characterization
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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 (494 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 (397 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
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (494 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 (397 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
2 Records (2 excluding Abstracts).
Total impact factor: 9.656 (9.656 excluding Abstracts).
Total 5 year impact factor: 10.244 (10.244 excluding Abstracts).
Total impact factor: 9.656 (9.656 excluding Abstracts).
Total 5 year impact factor: 10.244 (10.244 excluding Abstracts).
415 views. Last view on Thursday 03 March 2022, 21:18:46
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