The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.

Detalhes bibliográficos
Autor(a) principal: CASTRO, C. S. P. de
Data de Publicação: 2004
Outros Autores: SOUZADE, J. R., BLOCH JUNIOR, C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
Texto Completo: http://www.alice.cnptia.embrapa.br/alice/handle/doc/185340
Resumo: Binding of zinc to a 19 mer double-stranded oligodeoxyribonucleotide was investigated by anodic stripping voltammetry and cyclic voltammetry in order to understand the roles of zinc in DNA cleavage catalyzed by mung bean nuclease. These methods rely on the direct monitoring of zinc oxidation current in the absence and in the presence of the oligo. Zinc titration curves with the ds-oligodeoxyribonucleotide were obtained in concentrations ranging from 3.62×10-9 to 3.62×10-8 M and 4.06×10-10 to 5.25×10-9 M. The acquired data were used to determine the dissociation constant, stoichiometry and zinc binding sites of the complex and to understand the specific changes of ds-oligodeoxyribonucleotide secondary structure by zinc binding. The oxidation-reduction process of zinc was also investigated by cyclic voltammetry through I (oxidation current) versus v1/2 (square root of scan rate) curves in the absence and in the presence of the double-stranded oligodeoxyribonucleotide.
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spelling The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.Metodos eletroquímicosVoltametriaDNAZincoBinding of zinc to a 19 mer double-stranded oligodeoxyribonucleotide was investigated by anodic stripping voltammetry and cyclic voltammetry in order to understand the roles of zinc in DNA cleavage catalyzed by mung bean nuclease. These methods rely on the direct monitoring of zinc oxidation current in the absence and in the presence of the oligo. Zinc titration curves with the ds-oligodeoxyribonucleotide were obtained in concentrations ranging from 3.62×10-9 to 3.62×10-8 M and 4.06×10-10 to 5.25×10-9 M. The acquired data were used to determine the dissociation constant, stoichiometry and zinc binding sites of the complex and to understand the specific changes of ds-oligodeoxyribonucleotide secondary structure by zinc binding. The oxidation-reduction process of zinc was also investigated by cyclic voltammetry through I (oxidation current) versus v1/2 (square root of scan rate) curves in the absence and in the presence of the double-stranded oligodeoxyribonucleotide.2018-05-30T00:48:15Z2018-05-30T00:48:15Z2004-11-1720042018-05-30T00:48:15Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleBiophysical Chemistry, v.112, n. 1, p. 59-67, 2004.http://www.alice.cnptia.embrapa.br/alice/handle/doc/185340engCASTRO, C. S. P. deSOUZADE, J. R.BLOCH JUNIOR, C.info:eu-repo/semantics/openAccessreponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)instacron:EMBRAPA2018-05-30T00:48:22Zoai:www.alice.cnptia.embrapa.br:doc/185340Repositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestopendoar:21542018-05-30T00:48:22falseRepositório InstitucionalPUBhttps://www.alice.cnptia.embrapa.br/oai/requestcg-riaa@embrapa.bropendoar:21542018-05-30T00:48:22Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)false
dc.title.none.fl_str_mv The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
title The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
spellingShingle The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
CASTRO, C. S. P. de
Metodos eletroquímicos
Voltametria
DNA
Zinco
title_short The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
title_full The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
title_fullStr The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
title_full_unstemmed The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
title_sort The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
author CASTRO, C. S. P. de
author_facet CASTRO, C. S. P. de
SOUZADE, J. R.
BLOCH JUNIOR, C.
author_role author
author2 SOUZADE, J. R.
BLOCH JUNIOR, C.
author2_role author
author
dc.contributor.author.fl_str_mv CASTRO, C. S. P. de
SOUZADE, J. R.
BLOCH JUNIOR, C.
dc.subject.por.fl_str_mv Metodos eletroquímicos
Voltametria
DNA
Zinco
topic Metodos eletroquímicos
Voltametria
DNA
Zinco
description Binding of zinc to a 19 mer double-stranded oligodeoxyribonucleotide was investigated by anodic stripping voltammetry and cyclic voltammetry in order to understand the roles of zinc in DNA cleavage catalyzed by mung bean nuclease. These methods rely on the direct monitoring of zinc oxidation current in the absence and in the presence of the oligo. Zinc titration curves with the ds-oligodeoxyribonucleotide were obtained in concentrations ranging from 3.62×10-9 to 3.62×10-8 M and 4.06×10-10 to 5.25×10-9 M. The acquired data were used to determine the dissociation constant, stoichiometry and zinc binding sites of the complex and to understand the specific changes of ds-oligodeoxyribonucleotide secondary structure by zinc binding. The oxidation-reduction process of zinc was also investigated by cyclic voltammetry through I (oxidation current) versus v1/2 (square root of scan rate) curves in the absence and in the presence of the double-stranded oligodeoxyribonucleotide.
publishDate 2004
dc.date.none.fl_str_mv 2004-11-17
2004
2018-05-30T00:48:15Z
2018-05-30T00:48:15Z
2018-05-30T00:48:15Z
dc.type.driver.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv Biophysical Chemistry, v.112, n. 1, p. 59-67, 2004.
http://www.alice.cnptia.embrapa.br/alice/handle/doc/185340
identifier_str_mv Biophysical Chemistry, v.112, n. 1, p. 59-67, 2004.
url http://www.alice.cnptia.embrapa.br/alice/handle/doc/185340
dc.language.iso.fl_str_mv eng
language eng
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instname:Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron:EMBRAPA
instname_str Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
instacron_str EMBRAPA
institution EMBRAPA
reponame_str Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
collection Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice)
repository.name.fl_str_mv Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) - Empresa Brasileira de Pesquisa Agropecuária (Embrapa)
repository.mail.fl_str_mv cg-riaa@embrapa.br
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