Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex
Autor(a) principal: | |
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Data de Publicação: | 2010 |
Outros Autores: | , , , , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Journal of the Brazilian Chemical Society (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000700007 |
Resumo: | Catalytic promiscuity has emerged as an important property of many enzymes since the relationship of this property to enzymatic evolution became clear. Simultaneously, the development of suitable biomimetic catalytic systems capable of mimicking the promiscuous catalytic properties of such enzymes represents a new challenge for bioinorganic chemists. In this paper we report on the X-ray structure, the solution studies and the promiscuous catalytic activity of the mixed-valence complex [(bpbpmp)FeIII(µ-OAc)2FeII](ClO4), (1), containing the unsymmetrical dinucleating ligand 2-{[(2-hydroxybenzyl)(2-pyridylmethyl)aminomethyl]-4-methyl-6-[bis(2-pyridylmethyl)aminomethyl]}phenol (H2bpbpmp). Potentiometric and spectrophotometric titrations and kinetics studies showed that this coordination compound generates active species that promote hydrolytic cleavage of double strand DNA (dsDNA), with a rate enhancement of 1.9×10(8) over the non-catalyzed reaction, as well as promote oxidation of 3,5-di-tert-butylcatechol (3,5-dtbc), with k cat = 1.16 × 10-2 s-1 and K M = 7.1×10-4 mol L-1. Thus, complex 1 shows both hydrolase and oxidoreductase activities and can be regarded as a man-made model for studying catalytic promiscuity. |
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Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complexmixed-valence FeIII FeII complexunsymmetrical ligandcatalytic promiscuitydiester and DNA cleavagecatecholase activityCatalytic promiscuity has emerged as an important property of many enzymes since the relationship of this property to enzymatic evolution became clear. Simultaneously, the development of suitable biomimetic catalytic systems capable of mimicking the promiscuous catalytic properties of such enzymes represents a new challenge for bioinorganic chemists. In this paper we report on the X-ray structure, the solution studies and the promiscuous catalytic activity of the mixed-valence complex [(bpbpmp)FeIII(µ-OAc)2FeII](ClO4), (1), containing the unsymmetrical dinucleating ligand 2-{[(2-hydroxybenzyl)(2-pyridylmethyl)aminomethyl]-4-methyl-6-[bis(2-pyridylmethyl)aminomethyl]}phenol (H2bpbpmp). Potentiometric and spectrophotometric titrations and kinetics studies showed that this coordination compound generates active species that promote hydrolytic cleavage of double strand DNA (dsDNA), with a rate enhancement of 1.9×10(8) over the non-catalyzed reaction, as well as promote oxidation of 3,5-di-tert-butylcatechol (3,5-dtbc), with k cat = 1.16 × 10-2 s-1 and K M = 7.1×10-4 mol L-1. Thus, complex 1 shows both hydrolase and oxidoreductase activities and can be regarded as a man-made model for studying catalytic promiscuity.Sociedade Brasileira de Química2010-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000700007Journal of the Brazilian Chemical Society v.21 n.7 2010reponame:Journal of the Brazilian Chemical Society (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.1590/S0103-50532010000700007info:eu-repo/semantics/openAccessNeves,AdemirBortoluzzi,Adailton J.Jovito,RafaelPeralta,Rosely A.Souza,Bernardo deSzpoganicz,BrunoJoussef,Antônio C.Terenzi,HernánSeverino,Patricia C.Fischer,Franciele L.Schenk,GerhardRiley,Mark J.Smith,Sarah J.Gahan,Lawrence R.eng2010-07-30T00:00:00Zoai:scielo:S0103-50532010000700007Revistahttp://jbcs.sbq.org.brONGhttps://old.scielo.br/oai/scielo-oai.php||office@jbcs.sbq.org.br1678-47900103-5053opendoar:2010-07-30T00:00Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
title |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
spellingShingle |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex Neves,Ademir mixed-valence FeIII FeII complex unsymmetrical ligand catalytic promiscuity diester and DNA cleavage catecholase activity |
title_short |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
title_full |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
title_fullStr |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
title_full_unstemmed |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
title_sort |
Catalytic promiscuity: catecholase-like activity and hydrolytic DNA cleavage promoted by a mixed-valence FeIII FeII complex |
author |
Neves,Ademir |
author_facet |
Neves,Ademir Bortoluzzi,Adailton J. Jovito,Rafael Peralta,Rosely A. Souza,Bernardo de Szpoganicz,Bruno Joussef,Antônio C. Terenzi,Hernán Severino,Patricia C. Fischer,Franciele L. Schenk,Gerhard Riley,Mark J. Smith,Sarah J. Gahan,Lawrence R. |
author_role |
author |
author2 |
Bortoluzzi,Adailton J. Jovito,Rafael Peralta,Rosely A. Souza,Bernardo de Szpoganicz,Bruno Joussef,Antônio C. Terenzi,Hernán Severino,Patricia C. Fischer,Franciele L. Schenk,Gerhard Riley,Mark J. Smith,Sarah J. Gahan,Lawrence R. |
author2_role |
author author author author author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Neves,Ademir Bortoluzzi,Adailton J. Jovito,Rafael Peralta,Rosely A. Souza,Bernardo de Szpoganicz,Bruno Joussef,Antônio C. Terenzi,Hernán Severino,Patricia C. Fischer,Franciele L. Schenk,Gerhard Riley,Mark J. Smith,Sarah J. Gahan,Lawrence R. |
dc.subject.por.fl_str_mv |
mixed-valence FeIII FeII complex unsymmetrical ligand catalytic promiscuity diester and DNA cleavage catecholase activity |
topic |
mixed-valence FeIII FeII complex unsymmetrical ligand catalytic promiscuity diester and DNA cleavage catecholase activity |
description |
Catalytic promiscuity has emerged as an important property of many enzymes since the relationship of this property to enzymatic evolution became clear. Simultaneously, the development of suitable biomimetic catalytic systems capable of mimicking the promiscuous catalytic properties of such enzymes represents a new challenge for bioinorganic chemists. In this paper we report on the X-ray structure, the solution studies and the promiscuous catalytic activity of the mixed-valence complex [(bpbpmp)FeIII(µ-OAc)2FeII](ClO4), (1), containing the unsymmetrical dinucleating ligand 2-{[(2-hydroxybenzyl)(2-pyridylmethyl)aminomethyl]-4-methyl-6-[bis(2-pyridylmethyl)aminomethyl]}phenol (H2bpbpmp). Potentiometric and spectrophotometric titrations and kinetics studies showed that this coordination compound generates active species that promote hydrolytic cleavage of double strand DNA (dsDNA), with a rate enhancement of 1.9×10(8) over the non-catalyzed reaction, as well as promote oxidation of 3,5-di-tert-butylcatechol (3,5-dtbc), with k cat = 1.16 × 10-2 s-1 and K M = 7.1×10-4 mol L-1. Thus, complex 1 shows both hydrolase and oxidoreductase activities and can be regarded as a man-made model for studying catalytic promiscuity. |
publishDate |
2010 |
dc.date.none.fl_str_mv |
2010-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000700007 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0103-50532010000700007 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S0103-50532010000700007 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
publisher.none.fl_str_mv |
Sociedade Brasileira de Química |
dc.source.none.fl_str_mv |
Journal of the Brazilian Chemical Society v.21 n.7 2010 reponame:Journal of the Brazilian Chemical Society (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Journal of the Brazilian Chemical Society (Online) |
collection |
Journal of the Brazilian Chemical Society (Online) |
repository.name.fl_str_mv |
Journal of the Brazilian Chemical Society (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
||office@jbcs.sbq.org.br |
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1750318171065155584 |