Study of the binding of Eu3+ and Tb3+ to L-phenylalanine and L-tryptophan
Autor(a) principal: | |
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Data de Publicação: | 1997 |
Outros Autores: | , |
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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Repositório Institucional da UNESP |
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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 |
|
_version_ |
1808129543756578816 |