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Autore principale: Ana Maria Ferreira da Costa
Natura: Artículo científico
Lingua:en
Pubblicazione: Academia Brasileira de Ciências 2000
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Accesso online:https://www.redalyc.org/articulo.oa?id=32772107
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author Ana Maria Ferreira da Costa
author_facet Ana Maria Ferreira da Costa
contents Mimics of copper proteins: structural and functional aspects Ana Maria Ferreira da Costa Maria Lúcia Santos Pires dos Eleonice Maria Pereira Marcos Damasceno Oliveira Wendel Alves Andrade Multidisciplinaria (Ciencias Naturales y Exactas) EPR measurements copper protein mimics copper diimine complexes characterization and reactivity studies The importance of copper as an essential element can be estimated by the wide range of copper proteinsand enzymes playing different roles in biological systems. In the last decades many bioinorganic studieswere developed on mimetic complexes of copper-dependent proteins, in order to verify the interrelationsbetween structural and functional properties of active copper centers. Among the most studied copper ionligand, diimine compounds have deserved special attention due their flexibility, facility of preparation, andability to stabilize both oxidation states of this metal. In our laboratory, we have been investigating someSchiff base copper complexes as mimics of different proteins, with emphasis on functional aspects, trying toelucidate mechanisms of reaction, based on proposed intermediary species, in addition to molecular shapes.Particularly, mimics of the copper-zinc superoxide dismutase, and of monooxigenases and oxidases exhibitingdicopper sites are discussed in this work. 2000 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32772107 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.1 Vol.72
format Artículo científico
id redalyc_32772107
language en
publishDate 2000
publisher Academia Brasileira de Ciências
spellingShingle Mimics of copper proteins: structural and functional aspects
Ana Maria Ferreira da Costa
Multidisciplinaria (Ciencias Naturales y Exactas)
EPR measurements
copper protein mimics
copper diimine complexes
characterization and reactivity studies
Mimics of copper proteins: structural and functional aspects Ana Maria Ferreira da Costa Maria Lúcia Santos Pires dos Eleonice Maria Pereira Marcos Damasceno Oliveira Wendel Alves Andrade Multidisciplinaria (Ciencias Naturales y Exactas) EPR measurements copper protein mimics copper diimine complexes characterization and reactivity studies The importance of copper as an essential element can be estimated by the wide range of copper proteinsand enzymes playing different roles in biological systems. In the last decades many bioinorganic studieswere developed on mimetic complexes of copper-dependent proteins, in order to verify the interrelationsbetween structural and functional properties of active copper centers. Among the most studied copper ionligand, diimine compounds have deserved special attention due their flexibility, facility of preparation, andability to stabilize both oxidation states of this metal. In our laboratory, we have been investigating someSchiff base copper complexes as mimics of different proteins, with emphasis on functional aspects, trying toelucidate mechanisms of reaction, based on proposed intermediary species, in addition to molecular shapes.Particularly, mimics of the copper-zinc superoxide dismutase, and of monooxigenases and oxidases exhibitingdicopper sites are discussed in this work. 2000 artículo científico 0001-3765 https://www.redalyc.org/articulo.oa?id=32772107 en http://www.redalyc.org/revista.oa?id=327 Anais da Academia Brasileira de Ciências application/pdf Academia Brasileira de Ciências Anais da Academia Brasileira de Ciências (Brasil) Num.1 Vol.72
title Mimics of copper proteins: structural and functional aspects
topic Multidisciplinaria (Ciencias Naturales y Exactas)
EPR measurements
copper protein mimics
copper diimine complexes
characterization and reactivity studies
url https://www.redalyc.org/articulo.oa?id=32772107