Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan

Detalhes bibliográficos
Autor(a) principal: Carubelli, Célia R. [UNESP]
Data de Publicação: 1997
Outros Autores: Massabni, Ana M. G. [UNESP], Leite, Sergio R. de A. [UNESP]
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da UNESP
Texto Completo: http://dx.doi.org/10.1590/S0103-50531997000600006
http://hdl.handle.net/11449/65300
Resumo: Trivalent europium and terbium ions have ionic radii similar to that of Ca2+. So they are employed as probes of calcium binding sites in biological molecules. These ions exhibit very useful spectroscopic characteristics, chiefly a pronounced luminescence. In protein bound lanthanide, visible light emission from the lanthanide excited states can be observed when UV light is absorbed by aromatic amino acids. Subsequently, the energy is transferred to the lanthanide ion. The present work was carried out to define the binding sites of Eu3+ and Tb3+ in complexes with the aromatic amino acids L-phenylalanine and L-tryptophan. The techniques utilized were infrared and C nuclear magnetic resonance spectroscopies. It was found that trivalent europium and terbium interact with the carboxylate group of both amino acids. With L-tryptophan, the imino group of the indole ring is also involved representing another coordination site.
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spelling Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophanAromatic amino acidsLanthanidesTrivalent europium and terbium ions have ionic radii similar to that of Ca2+. So they are employed as probes of calcium binding sites in biological molecules. These ions exhibit very useful spectroscopic characteristics, chiefly a pronounced luminescence. In protein bound lanthanide, visible light emission from the lanthanide excited states can be observed when UV light is absorbed by aromatic amino acids. Subsequently, the energy is transferred to the lanthanide ion. The present work was carried out to define the binding sites of Eu3+ and Tb3+ in complexes with the aromatic amino acids L-phenylalanine and L-tryptophan. The techniques utilized were infrared and C nuclear magnetic resonance spectroscopies. It was found that trivalent europium and terbium interact with the carboxylate group of both amino acids. With L-tryptophan, the imino group of the indole ring is also involved representing another coordination site.Institute de Química Universidade Estadual Paulista, C.P. 355, 14801-970 Araraquara - SPInstitute de Química Universidade Estadual Paulista, C.P. 355, 14801-970 Araraquara - SPUniversidade Estadual Paulista (Unesp)Carubelli, Célia R. [UNESP]Massabni, Ana M. G. [UNESP]Leite, Sergio R. de A. [UNESP]2014-05-27T11:18:19Z2014-05-27T11:18:19Z1997-12-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article597-602application/pdfhttp://dx.doi.org/10.1590/S0103-50531997000600006Journal of the Brazilian Chemical Society, v. 8, n. 6, p. 597-602, 1997.0103-5053http://hdl.handle.net/11449/6530010.1590/S0103-50531997000600006S0103-50531997000600006WOS:0000726394000062-s2.0-00313304772-s2.0-0031330477.pdfScopusreponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of the Brazilian Chemical Society1.4440,357info:eu-repo/semantics/openAccess2024-01-22T06:25:49Zoai:repositorio.unesp.br:11449/65300Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-08-05T23:41:20.079822Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false
dc.title.none.fl_str_mv Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
title Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
spellingShingle Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
Carubelli, Célia R. [UNESP]
Aromatic amino acids
Lanthanides
title_short Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
title_full Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
title_fullStr Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
title_full_unstemmed Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
title_sort Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
author Carubelli, Célia R. [UNESP]
author_facet Carubelli, Célia R. [UNESP]
Massabni, Ana M. G. [UNESP]
Leite, Sergio R. de A. [UNESP]
author_role author
author2 Massabni, Ana M. G. [UNESP]
Leite, Sergio R. de A. [UNESP]
author2_role author
author
dc.contributor.none.fl_str_mv Universidade Estadual Paulista (Unesp)
dc.contributor.author.fl_str_mv Carubelli, Célia R. [UNESP]
Massabni, Ana M. G. [UNESP]
Leite, Sergio R. de A. [UNESP]
dc.subject.por.fl_str_mv Aromatic amino acids
Lanthanides
topic Aromatic amino acids
Lanthanides
description Trivalent europium and terbium ions have ionic radii similar to that of Ca2+. So they are employed as probes of calcium binding sites in biological molecules. These ions exhibit very useful spectroscopic characteristics, chiefly a pronounced luminescence. In protein bound lanthanide, visible light emission from the lanthanide excited states can be observed when UV light is absorbed by aromatic amino acids. Subsequently, the energy is transferred to the lanthanide ion. The present work was carried out to define the binding sites of Eu3+ and Tb3+ in complexes with the aromatic amino acids L-phenylalanine and L-tryptophan. The techniques utilized were infrared and C nuclear magnetic resonance spectroscopies. It was found that trivalent europium and terbium interact with the carboxylate group of both amino acids. With L-tryptophan, the imino group of the indole ring is also involved representing another coordination site.
publishDate 1997
dc.date.none.fl_str_mv 1997-12-01
2014-05-27T11:18:19Z
2014-05-27T11:18:19Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://dx.doi.org/10.1590/S0103-50531997000600006
Journal of the Brazilian Chemical Society, v. 8, n. 6, p. 597-602, 1997.
0103-5053
http://hdl.handle.net/11449/65300
10.1590/S0103-50531997000600006
S0103-50531997000600006
WOS:000072639400006
2-s2.0-0031330477
2-s2.0-0031330477.pdf
url http://dx.doi.org/10.1590/S0103-50531997000600006
http://hdl.handle.net/11449/65300
identifier_str_mv Journal of the Brazilian Chemical Society, v. 8, n. 6, p. 597-602, 1997.
0103-5053
10.1590/S0103-50531997000600006
S0103-50531997000600006
WOS:000072639400006
2-s2.0-0031330477
2-s2.0-0031330477.pdf
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Journal of the Brazilian Chemical Society
1.444
0,357
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 597-602
application/pdf
dc.source.none.fl_str_mv Scopus
reponame:Repositório Institucional da UNESP
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str Repositório Institucional da UNESP
collection Repositório Institucional da UNESP
repository.name.fl_str_mv Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv
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