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dc.contributor.author
Signorella, Sandra Rosanna  
dc.contributor.author
Palopoli, Claudia Marcela  
dc.contributor.author
Ledesma, Gabriela Nanci  
dc.date.available
2019-10-22T18:00:46Z  
dc.date.issued
2018-06  
dc.identifier.citation
Signorella, Sandra Rosanna; Palopoli, Claudia Marcela; Ledesma, Gabriela Nanci; Rationally designed mimics of antioxidant manganoenzymes: Role of structural features in the quest for catalysts with catalase and superoxide dismutase activity; Elsevier Science Sa; Coordination Chemistry Reviews; 365; 6-2018; 75-102  
dc.identifier.issn
0010-8545  
dc.identifier.uri
http://hdl.handle.net/11336/86937  
dc.description.abstract
Manganese catalases (MnCAT) and superoxide dismutases (MnSOD) deplete hydrogen peroxide and superoxide in cells through a ping-pong mechanism involving cyclic oxidation and reduction of the metal cofactor. In a variety of pathological situations, the generation of reactive oxygen species overwhelms the capacity of endogenous scavengers and tissues become vulnerable to damage. Due to the limited success of the use of exogenous SOD and CAT as therapeutic agents to reduce oxidative stress damage, investigations have been directed to the design of low molecular-weight antioxidant catalysts (SOD- or CAT-mimics). To disproportionate superoxide and hydrogen peroxide efficiently, the reduction potential of MnSOD and MnCAT is fine-tuned to values much lower than that of the Mn3+(aq)/Mn2+(aq) couple. In the artificial catalysts, the number and type of ligands, the local charge, the geometry around the metal, are among the factors that introduce a way of tuning the redox potential of Mn to face redox reactions. However structural and electronic factors affecting SOD activity do not parallel those controlling CAT activity. This review focus on synthetic mononuclear Mn complexes with SOD and/or CAT activity, stressing the role of ligand donor sites, endogenous acid/base groups, metal environment and second-sphere effects in the catalytic activity.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier Science Sa  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/  
dc.subject
CATALASE MIMICS  
dc.subject
MANGANESE COMPLEXES  
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STRUCTURE/ACTIVITY  
dc.subject
SUPEROXIDE DISMUTASE MIMICS  
dc.subject.classification
Química Inorgánica y Nuclear  
dc.subject.classification
Ciencias Químicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Rationally designed mimics of antioxidant manganoenzymes: Role of structural features in the quest for catalysts with catalase and superoxide dismutase activity  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2019-10-16T19:16:59Z  
dc.journal.volume
365  
dc.journal.pagination
75-102  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Signorella, Sandra Rosanna. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina  
dc.description.fil
Fil: Palopoli, Claudia Marcela. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina  
dc.description.fil
Fil: Ledesma, Gabriela Nanci. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Química Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Química Rosario; Argentina  
dc.journal.title
Coordination Chemistry Reviews  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0010854518300018  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.ccr.2018.03.005