Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization (615 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.828, 5-year impact factor: 5.122
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0030961554&partnerID=40&md5=b5f510958991e54605093a44acddd8ac
Keywords: Helical Structures, Heme Proteins, Iron, Peptides, Synthesis Design,
Affiliations:
Ctro. Interdipartimentale Ric. S., Ctro. Stud. Biocristallografia CNR, Via Mezzocannone 4, I-80134 Napoli, Italy
References:
Meunier, B., (1992) Chem. Rev., 92, pp. 1411-145
Mansuy, D., Battioni, P., Battioni, J.P., (1989) Eur. J. Biochem., 184, pp. 267-285
Mansuy, D., (1990) Pure Appl. Chem., 62, pp. 741-746
Collman, J.P., Zhang, X., Lee, V.J., Uffelman, E.S., Brauman, J.I., (1993) Science, 261, pp. 1404-1411
Buchler, J.W., Scharbert, B., (1988) J. Am. Chem. Soc., 110, pp. 4272-4276
Sessler, J.L., Wang, B., Harriman, A., (1993) J. Am. Chem. Soc., 115, pp. 10418-10419
Grennberg, H., Faizon, S., Backvall, J.E., (1993) Angew. Chem. Int. Ed. Engl., 32, pp. 263-264
Sun, L., Von Gersdorff, J., Niethammer, D., Tian, P., Kurreck, H., (1994) Angew. Chem. Int. Ed. Engl., 33, pp. 2318-2320
Collmann, J.P., Gagne, R.R., Reed, C.A., Halbert, T.R., Lang, G., Robinson, W.T., (1975) J. Am. Chem. Soc., 97, pp. 1427-1439
Traylor, T.G., Chang, C.K., Geibel, J., Berzinis, A., Mincey, T., Cannon, J., (1979) J. Am. Chem. Soc., 101, pp. 6716-6731
Suslick, K.S., Fox, M.M., (1983) J. Am. Chem. Soc., 105, pp. 3507-3510
Buchler, J.W., (1979) The Porphyrins, 1, pp. 389-483. , Ed.: D. Dolphin, Academic Press, New York
Adar, F., The Porphyrins, 3, pp. 167-209
Janson, T.R., Katz, J.J., The Porphyrins, 4, pp. 1-59
La Mar, G.N., Walker, F.A., The Porphyrins, 4, pp. 61-157
Dolphin, D., (1979) The Porphyrins, 7. , Academic Press, New York
Wuttke, D.S., Gray, H.B., (1993) Curr. Opin. Struct. Biol., 3, pp. 555-563
Tetreau, C., Lavalette, D., Momenteau, M., Fischer, J., Weiss, R., (1994) J. Am. Chem. Soc., 116, pp. 11840-11848
David, S., James, B.R., Dolphin, D., Traylor, T.G., Lopez, M., (1994) J. Am. Chem. Soc., 116, pp. 6-14
Lindsay Smith, J.R., (1994) Metalloporphyrins in Catalytic Oxidations, pp. 325-368. , Ed.: R. A. Sheldon, Marcel Dekker, New York
Adams, P.A., Byfield, M.P., De Milton, R.C.L., Pratt, J.M., (1988) J. Inorg. Biochem., 34, pp. 167-175
Mashino, T., Nakamura, S., Hirobe, M., (1990) Tetrahedron Lett., 31, pp. 3163-3166
Choma, C.T., Lear, J.D., Nelson, M.J., Dutton, P.L., Robertson, D.E., DeGrado, W.F., (1994) J. Am. Chem. Soc., 116, pp. 856-865
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
Sasaki, T., Kaiser, E.T., (1989) J. Am. Chem. Soc., 111, pp. 380-381
Casella, L., Gullotti, M., De Gioia, L., Monzani, E., Chillemi, F., (1991) J. Chem. Soc. Dalton Trans., pp. 2945-2953
Pispisa, B., Venanzi, M., D'Alagni, M., (1994) Biopolymers, 34, pp. 435-442
Ohkatsu, Y., Watanabe, T., Goto, T., Wakita, M., (1994) Bull. Chem. Soc. Jpn., 67, pp. 742-747
Benson, D.R., Hart, B.R., Zhu, X., Doughty, M.B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Nastri, F., Lombardi, A., Maglio, O., Morelli, G., D'Auria, G., Pavone, V., Pedone, C., (1994) Fourth Naples Workshop on Bioactive Peptides, p. 86. , Capri (Italy)
Lombardi, A., Nastri, F., Maglio, O., Morelli, G., Pavone, V., Pedone, C., Battioni, P., Chottard, G., (1994) Metal Ions in Biological Systems, Eurobic II, p. 218. , Florence (Italy)
Poulos, T.L., Finzel, B.C., Howard, A.J., (1986) Biochemistry, 25, pp. 5314-5322
Carter, D.C., Melis, K.A., O'Donnell, S.E., Burgess, B.K., Furey Jr., W.F., Wang, B.C., Stout, C.D., (1985) J. Mol. Biol., 184, pp. 279-295
Pierrot, M., Haser, R., Frey, M., Payan, F., Astier, J.P., (1982) J. Biol. Chem., 257, pp. 14341-14348
Mathews, F.S., Czerwinski, E.W., Argos, P., (1979) The Porphyrins, 7, pp. 108-146. , Ed.: D. Dolphin, Academic Press, New York
Perutz, M.F., Hasnain, S.S., Duke, P.J., Sessler, J.L., Hahn, J.E., (1982) Nature, 295, pp. 535-538
Phillips, S.E.V., (1980) J. Mol. Biol., 142, pp. 531-554
Finzel, B.C., Weber, P.C., Hardman, K.D., Salemme, F.R., (1985) J. Mol. Biol., 186, pp. 627-643
Lederer, F., Glatigny, A., Bethge, P.H., Bellamy, H.D., Mathews, F.S., (1981) J. Mol. Biol., 148, pp. 427-448
O'Neil, K.T., DeGrado, W.F., (1990) Science, 250, pp. 646-651
Creamer, T.P., Rose, G.D., (1994) Proteins: Structure, Function and Genetics, 19, pp. 85-97
Serrano, L., Fersht, A.R., (1989) Nature, 342, pp. 296-299
Dryland, A., Sheppard, R.C., (1986) J. Chem. Soc. Perkin Trans. I, pp. 125-137
Coste, J., Le-Nguyen, D., Castro, B., (1990) Tetrahedron Lett., 31, pp. 205-208
Kaiser, E., Colescott, R.L., Biossinger, C.D., Cook, P.I., (1970) Anal. Biochem., 34, pp. 595-598
Bycroft, B.W., Chan, W.C., Chhabra, S.R., Hone, N.D., (1993) J. Chem. Soc. Chem. Commun., pp. 778-779
Adar, F., (1979) The Porphyrins, 3, pp. 167-209. , Ed.: D. Dolphin, Academic Press, New York
Warme, P.K., Hager, L.P., (1970) Biochemistry, 9, pp. 1606-1614
Babcock, G.T., Widger, W.R., Cramer, W.A., Oertling, W.A., Metz, J.G., (1985) Biochemistry, 24, pp. 3638-3645
Brault, D., Rougee, M., (1974) Biochemistry, 13, pp. 4591-4602
Greenfield, N., Fasman, G.D., (1969) Biochemistry, 8, pp. 4108-4116
Oekonomopoulos, R., Jung, G., (1980) Biopolymers, 19, pp. 203-214
Sudha, T.S., Yijayakumar, E.K.S., Balaram, P., (1983) Int. J. Peptide Protein Res., 22, pp. 464-468
Mutter, M., Altmann, K.H., Florsheimer, A., Herbert, J., (1986) Helv. Chim. Acta, 69, pp. 786-792
Manning, M.C., Woody, R.W., (1991) Biopolymers, 31, pp. 569-586
Vuilleumier, S., Mutter, M., (1993) Biopolymers, 33, pp. 389-400
Nakano, M., Iwamaru, H., Tobita, T., (1982) Biopolymers, 21, pp. 805-815
Sonnichsen, F.D., Van Eyk, J.E., Hodges, R.S., Sykes, B.D., (1992) Biochemistry, 31, pp. 8790-8798
Storrs, R.W., Truckses, D., Wemmer, D.E., (1992) Biopolymers, 32, pp. 1695-1702
Jasanoff, A., Fersht, A.R., (1994) Biochemistry, 33, pp. 2129-2135
Cammers-Goodwin, A., Allen, T.J., Oslick, S.L., McClure, K.F., Lee, J.H., Kemp, D.S., (1996) J. Am. Chem. Soc., 118, pp. 3082-3090
Myer, Y.P., Pande, A., (1978) The Porphyrins, 4, pp. 271-321. , Ed.: D. Dolphin, Academic Press, New York
Myer, Y.P., (1978) Methods Enzymol., 54, pp. 249-284
Hsu, M.-C., Woody, R.W., (1971) J. Am. Chem. Soc., 93, pp. 3515-3523
Nicola, N.A., Minasian, E., Appleby, C.A., Leach, S.J., (1975) Biochemistry, 14, pp. 5141-5149
Myer, Y.P., (1968) J. Biol. Chem., 243, pp. 2115-2122
Bullock, P.A., Myer, Y.P., (1978) Biochemistry, 17, pp. 3084-3091
Abola, E.E., Bernstein, F.C., Bryant, S.H., Koetzle, T.F., Weng, J., (1987) Data Commission of the International Union of Crystallography, pp. 107-132. , F. H. Allen, G. Bergerhoff, R. Sievers, Bonn/Cambridge/Chester
Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer Jr., E.F., Brice, M.D., Rodgers, J.R., Kennard, O., Tasumi, M., (1987) J. Mol. Biol., 112, pp. 535-542
Johnson Jr., W.C., (1985) Methods Biochem. Anal., 31, pp. 61-163
Collman, J. P., Zhang, X., Lee, V. J., Uffelman, E. S., Brauman, J. I., (1993) Science, 261, pp. 1404-1411
Buchler, J. W., Scharbert, B., (1988) J. Am. Chem. Soc., 110, pp. 4272-4276
Sessler, J. L., Wang, B., Harriman, A., (1993) J. Am. Chem. Soc., 115, pp. 10418-10419
Collmann, J. P., Gagne, R. R., Reed, C. A., Halbert, T. R., Lang, G., Robinson, W. T., (1975) J. Am. Chem. Soc., 97, pp. 1427-1439
Traylor, T. G., Chang, C. K., Geibel, J., Berzinis, A., Mincey, T., Cannon, J., (1979) J. Am. Chem. Soc., 101, pp. 6716-6731
Suslick, K. S., Fox, M. M., (1983) J. Am. Chem. Soc., 105, pp. 3507-3510
Buchler, J. W., (1979) The Porphyrins, 1, pp. 389-483. , Ed.: D. Dolphin, Academic Press, New York
Janson, T. R., Katz, J. J., The Porphyrins, 4, pp. 1-59
La Mar, G. N., Walker, F. A., The Porphyrins, 4, pp. 61-157
Wuttke, D. S., Gray, H. B., (1993) Curr. Opin. Struct. Biol., 3, pp. 555-563
Lindsay Smith, J. R., (1994) Metalloporphyrins in Catalytic Oxidations, pp. 325-368. , Ed.: R. A. Sheldon, Marcel Dekker, New York
Adams, P. A., Byfield, M. P., De Milton, R. C. L., Pratt, J. M., (1988) J. Inorg. Biochem., 34, pp. 167-175
Choma, C. T., Lear, J. D., Nelson, M. J., Dutton, P. L., Robertson, D. E., DeGrado, W. F., (1994) J. Am. Chem. Soc., 116, pp. 856-865
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
Benson, D. R., Hart, B. R., Zhu, X., Doughty, M. B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Poulos, T. L., Finzel, B. C., Howard, A. J., (1986) Biochemistry, 25, pp. 5314-5322
Carter, D. C., Melis, K. A., O'Donnell, S. E., Burgess, B. K., Furey Jr., W. F., Wang, B. C., Stout, C. D., (1985) J. Mol. Biol., 184, pp. 279-295
Mathews, F. S., Czerwinski, E. W., Argos, P., (1979) The Porphyrins, 7, pp. 108-146. , Ed.: D. Dolphin, Academic Press, New York
Perutz, M. F., Hasnain, S. S., Duke, P. J., Sessler, J. L., Hahn, J. E., (1982) Nature, 295, pp. 535-538
Phillips, S. E. V., (1980) J. Mol. Biol., 142, pp. 531-554
Finzel, B. C., Weber, P. C., Hardman, K. D., Salemme, F. R., (1985) J. Mol. Biol., 186, pp. 627-643
O'Neil, K. T., DeGrado, W. F., (1990) Science, 250, pp. 646-651
Creamer, T. P., Rose, G. D., (1994) Proteins: Structure, Function and Genetics, 19, pp. 85-97
Bycroft, B. W., Chan, W. C., Chhabra, S. R., Hone, N. D., (1993) J. Chem. Soc. Chem. Commun., pp. 778-779
Warme, P. K., Hager, L. P., (1970) Biochemistry, 9, pp. 1606-1614
Babcock, G. T., Widger, W. R., Cramer, W. A., Oertling, W. A., Metz, J. G., (1985) Biochemistry, 24, pp. 3638-3645
Sudha, T. S., Yijayakumar, E. K. S., Balaram, P., (1983) Int. J. Peptide Protein Res., 22, pp. 464-468
Manning, M. C., Woody, R. W., (1991) Biopolymers, 31, pp. 569-586
Sonnichsen, F. D., Van Eyk, J. E., Hodges, R. S., Sykes, B. D., (1992) Biochemistry, 31, pp. 8790-8798
Storrs, R. W., Truckses, D., Wemmer, D. E., (1992) Biopolymers, 32, pp. 1695-1702
Myer, Y. P., Pande, A., (1978) The Porphyrins, 4, pp. 271-321. , Ed.: D. Dolphin, Academic Press, New York
Myer, Y. P., (1978) Methods Enzymol., 54, pp. 249-284
Hsu, M. -C., Woody, R. W., (1971) J. Am. Chem. Soc., 93, pp. 3515-3523
Nicola, N. A., Minasian, E., Appleby, C. A., Leach, S. J., (1975) Biochemistry, 14, pp. 5141-5149
Myer, Y. P., (1968) J. Biol. Chem., 243, pp. 2115-2122
Bullock, P. A., Myer, Y. P., (1978) Biochemistry, 17, pp. 3084-3091
Abola, E. E., Bernstein, F. C., Bryant, S. H., Koetzle, T. F., Weng, J., (1987) Data Commission of the International Union of Crystallography, pp. 107-132. , F. H. Allen, G. Bergerhoff, R. Sievers, Bonn/Cambridge/Chester
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer Jr., E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Tasumi, M., (1987) J. Mol. Biol., 112, pp. 535-542
Johnson Jr., W. C., (1985) Methods Biochem. Anal., 31, pp. 61-163
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1997; 3(3): 340-349.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 4.828, 5-year impact factor: 5.122
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0030961554&partnerID=40&md5=b5f510958991e54605093a44acddd8ac
Keywords: Helical Structures, Heme Proteins, Iron, Peptides, Synthesis Design,
Affiliations:
Ctro. Interdipartimentale Ric. S., Ctro. Stud. Biocristallografia CNR, Via Mezzocannone 4, I-80134 Napoli, Italy
References:
Meunier, B., (1992) Chem. Rev., 92, pp. 1411-145
Mansuy, D., Battioni, P., Battioni, J.P., (1989) Eur. J. Biochem., 184, pp. 267-285
Mansuy, D., (1990) Pure Appl. Chem., 62, pp. 741-746
Collman, J.P., Zhang, X., Lee, V.J., Uffelman, E.S., Brauman, J.I., (1993) Science, 261, pp. 1404-1411
Buchler, J.W., Scharbert, B., (1988) J. Am. Chem. Soc., 110, pp. 4272-4276
Sessler, J.L., Wang, B., Harriman, A., (1993) J. Am. Chem. Soc., 115, pp. 10418-10419
Grennberg, H., Faizon, S., Backvall, J.E., (1993) Angew. Chem. Int. Ed. Engl., 32, pp. 263-264
Sun, L., Von Gersdorff, J., Niethammer, D., Tian, P., Kurreck, H., (1994) Angew. Chem. Int. Ed. Engl., 33, pp. 2318-2320
Collmann, J.P., Gagne, R.R., Reed, C.A., Halbert, T.R., Lang, G., Robinson, W.T., (1975) J. Am. Chem. Soc., 97, pp. 1427-1439
Traylor, T.G., Chang, C.K., Geibel, J., Berzinis, A., Mincey, T., Cannon, J., (1979) J. Am. Chem. Soc., 101, pp. 6716-6731
Suslick, K.S., Fox, M.M., (1983) J. Am. Chem. Soc., 105, pp. 3507-3510
Buchler, J.W., (1979) The Porphyrins, 1, pp. 389-483. , Ed.: D. Dolphin, Academic Press, New York
Adar, F., The Porphyrins, 3, pp. 167-209
Janson, T.R., Katz, J.J., The Porphyrins, 4, pp. 1-59
La Mar, G.N., Walker, F.A., The Porphyrins, 4, pp. 61-157
Dolphin, D., (1979) The Porphyrins, 7. , Academic Press, New York
Wuttke, D.S., Gray, H.B., (1993) Curr. Opin. Struct. Biol., 3, pp. 555-563
Tetreau, C., Lavalette, D., Momenteau, M., Fischer, J., Weiss, R., (1994) J. Am. Chem. Soc., 116, pp. 11840-11848
David, S., James, B.R., Dolphin, D., Traylor, T.G., Lopez, M., (1994) J. Am. Chem. Soc., 116, pp. 6-14
Lindsay Smith, J.R., (1994) Metalloporphyrins in Catalytic Oxidations, pp. 325-368. , Ed.: R. A. Sheldon, Marcel Dekker, New York
Adams, P.A., Byfield, M.P., De Milton, R.C.L., Pratt, J.M., (1988) J. Inorg. Biochem., 34, pp. 167-175
Mashino, T., Nakamura, S., Hirobe, M., (1990) Tetrahedron Lett., 31, pp. 3163-3166
Choma, C.T., Lear, J.D., Nelson, M.J., Dutton, P.L., Robertson, D.E., DeGrado, W.F., (1994) J. Am. Chem. Soc., 116, pp. 856-865
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
Sasaki, T., Kaiser, E.T., (1989) J. Am. Chem. Soc., 111, pp. 380-381
Casella, L., Gullotti, M., De Gioia, L., Monzani, E., Chillemi, F., (1991) J. Chem. Soc. Dalton Trans., pp. 2945-2953
Pispisa, B., Venanzi, M., D'Alagni, M., (1994) Biopolymers, 34, pp. 435-442
Ohkatsu, Y., Watanabe, T., Goto, T., Wakita, M., (1994) Bull. Chem. Soc. Jpn., 67, pp. 742-747
Benson, D.R., Hart, B.R., Zhu, X., Doughty, M.B., (1995) J. Am. Chem. Soc., 117, pp. 8502-8510
Nastri, F., Lombardi, A., Maglio, O., Morelli, G., D'Auria, G., Pavone, V., Pedone, C., (1994) Fourth Naples Workshop on Bioactive Peptides, p. 86. , Capri (Italy)
Lombardi, A., Nastri, F., Maglio, O., Morelli, G., Pavone, V., Pedone, C., Battioni, P., Chottard, G., (1994) Metal Ions in Biological Systems, Eurobic II, p. 218. , Florence (Italy)
Poulos, T.L., Finzel, B.C., Howard, A.J., (1986) Biochemistry, 25, pp. 5314-5322
Carter, D.C., Melis, K.A., O'Donnell, S.E., Burgess, B.K., Furey Jr., W.F., Wang, B.C., Stout, C.D., (1985) J. Mol. Biol., 184, pp. 279-295
Pierrot, M., Haser, R., Frey, M., Payan, F., Astier, J.P., (1982) J. Biol. Chem., 257, pp. 14341-14348
Mathews, F.S., Czerwinski, E.W., Argos, P., (1979) The Porphyrins, 7, pp. 108-146. , Ed.: D. Dolphin, Academic Press, New York
Perutz, M.F., Hasnain, S.S., Duke, P.J., Sessler, J.L., Hahn, J.E., (1982) Nature, 295, pp. 535-538
Phillips, S.E.V., (1980) J. Mol. Biol., 142, pp. 531-554
Finzel, B.C., Weber, P.C., Hardman, K.D., Salemme, F.R., (1985) J. Mol. Biol., 186, pp. 627-643
Lederer, F., Glatigny, A., Bethge, P.H., Bellamy, H.D., Mathews, F.S., (1981) J. Mol. Biol., 148, pp. 427-448
O'Neil, K.T., DeGrado, W.F., (1990) Science, 250, pp. 646-651
Creamer, T.P., Rose, G.D., (1994) Proteins: Structure, Function and Genetics, 19, pp. 85-97
Serrano, L., Fersht, A.R., (1989) Nature, 342, pp. 296-299
Dryland, A., Sheppard, R.C., (1986) J. Chem. Soc. Perkin Trans. I, pp. 125-137
Coste, J., Le-Nguyen, D., Castro, B., (1990) Tetrahedron Lett., 31, pp. 205-208
Kaiser, E., Colescott, R.L., Biossinger, C.D., Cook, P.I., (1970) Anal. Biochem., 34, pp. 595-598
Bycroft, B.W., Chan, W.C., Chhabra, S.R., Hone, N.D., (1993) J. Chem. Soc. Chem. Commun., pp. 778-779
Adar, F., (1979) The Porphyrins, 3, pp. 167-209. , Ed.: D. Dolphin, Academic Press, New York
Warme, P.K., Hager, L.P., (1970) Biochemistry, 9, pp. 1606-1614
Babcock, G.T., Widger, W.R., Cramer, W.A., Oertling, W.A., Metz, J.G., (1985) Biochemistry, 24, pp. 3638-3645
Brault, D., Rougee, M., (1974) Biochemistry, 13, pp. 4591-4602
Greenfield, N., Fasman, G.D., (1969) Biochemistry, 8, pp. 4108-4116
Oekonomopoulos, R., Jung, G., (1980) Biopolymers, 19, pp. 203-214
Sudha, T.S., Yijayakumar, E.K.S., Balaram, P., (1983) Int. J. Peptide Protein Res., 22, pp. 464-468
Mutter, M., Altmann, K.H., Florsheimer, A., Herbert, J., (1986) Helv. Chim. Acta, 69, pp. 786-792
Manning, M.C., Woody, R.W., (1991) Biopolymers, 31, pp. 569-586
Vuilleumier, S., Mutter, M., (1993) Biopolymers, 33, pp. 389-400
Nakano, M., Iwamaru, H., Tobita, T., (1982) Biopolymers, 21, pp. 805-815
Sonnichsen, F.D., Van Eyk, J.E., Hodges, R.S., Sykes, B.D., (1992) Biochemistry, 31, pp. 8790-8798
Storrs, R.W., Truckses, D., Wemmer, D.E., (1992) Biopolymers, 32, pp. 1695-1702
Jasanoff, A., Fersht, A.R., (1994) Biochemistry, 33, pp. 2129-2135
Cammers-Goodwin, A., Allen, T.J., Oslick, S.L., McClure, K.F., Lee, J.H., Kemp, D.S., (1996) J. Am. Chem. Soc., 118, pp. 3082-3090
Myer, Y.P., Pande, A., (1978) The Porphyrins, 4, pp. 271-321. , Ed.: D. Dolphin, Academic Press, New York
Myer, Y.P., (1978) Methods Enzymol., 54, pp. 249-284
Hsu, M.-C., Woody, R.W., (1971) J. Am. Chem. Soc., 93, pp. 3515-3523
Nicola, N.A., Minasian, E., Appleby, C.A., Leach, S.J., (1975) Biochemistry, 14, pp. 5141-5149
Myer, Y.P., (1968) J. Biol. Chem., 243, pp. 2115-2122
Bullock, P.A., Myer, Y.P., (1978) Biochemistry, 17, pp. 3084-3091
Abola, E.E., Bernstein, F.C., Bryant, S.H., Koetzle, T.F., Weng, J., (1987) Data Commission of the International Union of Crystallography, pp. 107-132. , F. H. Allen, G. Bergerhoff, R. Sievers, Bonn/Cambridge/Chester
Bernstein, F.C., Koetzle, T.F., Williams, G.J.B., Meyer Jr., E.F., Brice, M.D., Rodgers, J.R., Kennard, O., Tasumi, M., (1987) J. Mol. Biol., 112, pp. 535-542
Johnson Jr., W.C., (1985) Methods Biochem. Anal., 31, pp. 61-163
Collman, J. P., Zhang, X., Lee, V. J., Uffelman, E. S., Brauman, J. I., (1993) Science, 261, pp. 1404-1411
Buchler, J. W., Scharbert, B., (1988) J. Am. Chem. Soc., 110, pp. 4272-4276
Sessler, J. L., Wang, B., Harriman, A., (1993) J. Am. Chem. Soc., 115, pp. 10418-10419
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Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization
In this paper we describe the design, synthesis, and spectroscopic characterization of a covalent helix heme helix sandwich named Fe(III) mimochrome I. It contains deuterohemin bound through both propionyl groups to two identical N- and C-terminal protected nonapeptides as α-helical scaffolds. Each peptide moiety bears a His residue in the central position, which acts as axial ligand to the metal ion. The newly developed synthetic strategy is based on a combination of solution and solid-phase methodologies. It represents a powerful method for obtaining a large variety of analogues containing two symmetric or unsymmetric peptide chains covalently bound to the deuteroporphyrin ring. UV Visible spectroscopic characterization in buffered 2,2,2,-trifluoroethanol water solution proves low-spin bis(histidine) iron(III) coordination; circular dichroism (CD) measurements show an α-helical conformation for the peptide moieties. Thus, all the data are in agreement with the designed hypothetical model regarding both the iron(III) coordination and the peptide chain structural organization.
In this paper we describe the design, synthesis, and spectroscopic characterization of a covalent helix heme helix sandwich named Fe(III) mimochrome I. It contains deuterohemin bound through both propionyl groups to two identical N- and C-terminal protected nonapeptides as α-helical scaffolds. Each peptide moiety bears a His residue in the central position, which acts as axial ligand to the metal ion. The newly developed synthetic strategy is based on a combination of solution and solid-phase methodologies. It represents a powerful method for obtaining a large variety of analogues containing two symmetric or unsymmetric peptide chains covalently bound to the deuteroporphyrin ring. UV Visible spectroscopic characterization in buffered 2,2,2,-trifluoroethanol water solution proves low-spin bis(histidine) iron(III) coordination; circular dichroism (CD) measurements show an α-helical conformation for the peptide moieties. Thus, all the data are in agreement with the designed hypothetical model regarding both the iron(III) coordination and the peptide chain structural organization.
Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization
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Hemoprotein models based on a covalent helix-heme-helix sandwich: 1. Design, synthesis, and characterization
Other filter: ([btitle,keywords] "Helical Structures" ...
Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
* Exploring the ability of cyclic peptides to target SAM domains: a computational and experimental study (266 views)
Chembiochem (ISSN: 1439-4227linking, 1439-7633), 2020 Mar 2; 21(5): 702-711.
Impact Factor: 2.641
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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
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Chino M, Maglio O, Nastri F, Pavone V, Degrado WF, Lombardi A
* Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (640 views)
Eur J Inorg Chem (ISSN: 1434-1948, 1099-0682e), 2015; 2015(21): 3371-3390.
Impact Factor: 2.686
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Pannuzzo M, Raudino A, Milardi D, La Rosa C, Karttunen M
* α-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (753 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2013; 3: N/D-N/D.
Impact Factor: 5.078
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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 (450 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Impact Factor: 5.925
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La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1135 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
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Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
* Structural determinants of the unusual helix stability of a de novo engineered vascular endothelial growth factor (VEGF) mimicking peptide (470 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2008; 14(14): 4164-4166.
Impact Factor: 5.454
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Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (432 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
Impact Factor: 4.907
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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 (379 views)
J Biol Inorg Chem (ISSN: 0949-8257, 1432-1327electronic, 0949-8257print), 2004 Dec; 9(8): 1017-1027.
Impact Factor: 3.3
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Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
* Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue (387 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Apr 2; 5(4): 541-544.
Impact Factor: 3.474
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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
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Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (384 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
View Export to BibTeX Export to EndNote
Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (491 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
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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 (489 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] (363 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
View Export to BibTeX Export to EndNote
* Exploring the ability of cyclic peptides to target SAM domains: a computational and experimental study (266 views)
Chembiochem (ISSN: 1439-4227linking, 1439-7633), 2020 Mar 2; 21(5): 702-711.
Impact Factor: 2.641
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, Maglio O, Nastri F, Pavone V, Degrado WF, Lombardi A
* Artificial Diiron Enzymes with a de Novo Designed Four-Helix Bundle Structure (640 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
Pannuzzo M, Raudino A, Milardi D, La Rosa C, Karttunen M
* α-Helical structures drive early stages of self-assembly of amyloidogenic amyloid polypeptide aggregate formation in membranes (753 views)
Sci Rep (ISSN: 2045-2322, 2045-2322electronic, 2045-2322linking), 2013; 3: N/D-N/D.
Impact Factor: 5.078
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 (450 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
La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1135 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
View Export to BibTeX Export to EndNote
Diana D, Ziaco B, Colombo G, Scarabelli G, Romanelli A, Fedone C, Fattorusso R, D'Andrea LD
* Structural determinants of the unusual helix stability of a de novo engineered vascular endothelial growth factor (VEGF) mimicking peptide (470 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2008; 14(14): 4164-4166.
Impact Factor: 5.454
View Export to BibTeX Export to EndNote
Grasso D, Grasso G, Guantieri V, Impellizzeri G, La Rosa C, Milardi D, Micera G, Osz K, Pappalardo G, Rizzarelli E, Sanna D, Sovago I
* Environmental effects on a prion's helix II domain: copper(II) and membrane interactions with PrP180-193 and its analogues (432 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2005 Dec 23; 12(2): 537-547.
Impact Factor: 4.907
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 (379 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
Saviano M, Improta R, Benedetti E, Carrozzini B, Cascarano GL, Didierjean C, Toniolo C, Crisma M
* Benzophenone photophore flexibility and proximity: Molecular and crystal-state structure of a Bpa-containing trichogin dodecapeptide analogue (387 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2004 Apr 2; 5(4): 541-544.
Impact Factor: 3.474
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
Carotenuto L, Berisio R, Piccolo C, Vitagliano L, Zagari A
* Video observation of protein crystal growth in the advanced protein crystallization facility aboard the space shuttle mission STS-95 (384 views)
J Cryst Growth (ISSN: 0022-0248), 2001; 232(1-4): 481-488.
Impact Factor: 1.283
View Export to BibTeX Export to EndNote
Impellizzeri G, Pappalardo G, Purrello R, Rizzarelli E, Santoro AM
Synthesis, spectroscopic characterisation, and metal ion interaction of a new α-helical peptide (491 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 1998; 4(9): 1791-1798.
Impact Factor: 5.153
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 (489 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] (363 views)
Lancet (ISSN: 0140-6736), 1996 Mar 30; 347(9005): 900-900.
Impact Factor: 16.135
View Export to BibTeX Export to EndNote
15 Records (13 excluding Abstracts).
Total impact factor: 73.467 (52.254 excluding Abstracts).
Total 5 year impact factor: 82.084 (52.805 excluding Abstracts).
Total impact factor: 73.467 (52.254 excluding Abstracts).
Total 5 year impact factor: 82.084 (52.805 excluding Abstracts).
615 views. Last view on Tuesday 30 May 2023, 0:56:19
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