The binding of zinc (II) to a double-stranded oligodeoxyribonucleotide; a voltammetric study.
Autor(a) principal: | |
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Data de Publicação: | 2004 |
Outros Autores: | , |
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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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 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA - Alice) 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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1794503455474188288 |