IMIDAZOL E CATÁLISE: UM PAR PERFEITO
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | por |
Título da fonte: | Química Nova (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422021000300318 |
Resumo: | The imidazole (IMZ) ring presents several chemical properties that turns it into a versatile acid-basic/nucleophilic catalyst. The discovery of the biological properties of histidine (amino acid with IMZ ring) instigates the study of this class of compounds. It is found in nature in several enzymes such as chymotrypsin and RNAses due to these properties. This review is focused on the catalytic role of IMZ towards the cleavage of acyl and phosphate esters and is structured in the following topics: chemical properties, biological catalysis (RNAses, phosphohistidines, chymotrypsin), intermolecular and intramolecular catalytic models and polymer and nanomaterials-based catalysts. Besides we discuss some properties such as tautomerism, stability, basicity and spectroscopic behavior, correlating with its reactivity in deacylation and dephosphorylation reactions. The main reaction mechanisms and kinetics promoted by IMZ as an acid, basic and nucleophilic catalysts are explored showing some examples. In addition, the importance of IMZ in enzymatic sites and their mechanisms and further combining properties of IMZ with some materials such as (bio)polymers, graphene, and cyclodextrines are covered. In this sense, with the wide IMZ data presented here, we are evidencing the perfect match between IMZ and catalysis. |
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IMIDAZOL E CATÁLISE: UM PAR PERFEITOreaction mechanismsdeacylationdephoshorylationorganophosphatesenzymatic modelsThe imidazole (IMZ) ring presents several chemical properties that turns it into a versatile acid-basic/nucleophilic catalyst. The discovery of the biological properties of histidine (amino acid with IMZ ring) instigates the study of this class of compounds. It is found in nature in several enzymes such as chymotrypsin and RNAses due to these properties. This review is focused on the catalytic role of IMZ towards the cleavage of acyl and phosphate esters and is structured in the following topics: chemical properties, biological catalysis (RNAses, phosphohistidines, chymotrypsin), intermolecular and intramolecular catalytic models and polymer and nanomaterials-based catalysts. Besides we discuss some properties such as tautomerism, stability, basicity and spectroscopic behavior, correlating with its reactivity in deacylation and dephosphorylation reactions. The main reaction mechanisms and kinetics promoted by IMZ as an acid, basic and nucleophilic catalysts are explored showing some examples. In addition, the importance of IMZ in enzymatic sites and their mechanisms and further combining properties of IMZ with some materials such as (bio)polymers, graphene, and cyclodextrines are covered. In this sense, with the wide IMZ data presented here, we are evidencing the perfect match between IMZ and catalysis.Sociedade Brasileira de Química2021-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422021000300318Química Nova v.44 n.3 2021reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.21577/0100-4042.20170659info:eu-repo/semantics/openAccessSilva,Valmir B.Orth,Elisa S.por2021-05-21T00:00:00Zoai:scielo:S0100-40422021000300318Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2021-05-21T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false |
dc.title.none.fl_str_mv |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
title |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
spellingShingle |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO Silva,Valmir B. reaction mechanisms deacylation dephoshorylation organophosphates enzymatic models |
title_short |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
title_full |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
title_fullStr |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
title_full_unstemmed |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
title_sort |
IMIDAZOL E CATÁLISE: UM PAR PERFEITO |
author |
Silva,Valmir B. |
author_facet |
Silva,Valmir B. Orth,Elisa S. |
author_role |
author |
author2 |
Orth,Elisa S. |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Silva,Valmir B. Orth,Elisa S. |
dc.subject.por.fl_str_mv |
reaction mechanisms deacylation dephoshorylation organophosphates enzymatic models |
topic |
reaction mechanisms deacylation dephoshorylation organophosphates enzymatic models |
description |
The imidazole (IMZ) ring presents several chemical properties that turns it into a versatile acid-basic/nucleophilic catalyst. The discovery of the biological properties of histidine (amino acid with IMZ ring) instigates the study of this class of compounds. It is found in nature in several enzymes such as chymotrypsin and RNAses due to these properties. This review is focused on the catalytic role of IMZ towards the cleavage of acyl and phosphate esters and is structured in the following topics: chemical properties, biological catalysis (RNAses, phosphohistidines, chymotrypsin), intermolecular and intramolecular catalytic models and polymer and nanomaterials-based catalysts. Besides we discuss some properties such as tautomerism, stability, basicity and spectroscopic behavior, correlating with its reactivity in deacylation and dephosphorylation reactions. The main reaction mechanisms and kinetics promoted by IMZ as an acid, basic and nucleophilic catalysts are explored showing some examples. In addition, the importance of IMZ in enzymatic sites and their mechanisms and further combining properties of IMZ with some materials such as (bio)polymers, graphene, and cyclodextrines are covered. In this sense, with the wide IMZ data presented here, we are evidencing the perfect match between IMZ and catalysis. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-03-01 |
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=S0100-40422021000300318 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422021000300318 |
dc.language.iso.fl_str_mv |
por |
language |
por |
dc.relation.none.fl_str_mv |
10.21577/0100-4042.20170659 |
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 |
Química Nova v.44 n.3 2021 reponame:Química Nova (Online) instname:Sociedade Brasileira de Química (SBQ) instacron:SBQ |
instname_str |
Sociedade Brasileira de Química (SBQ) |
instacron_str |
SBQ |
institution |
SBQ |
reponame_str |
Química Nova (Online) |
collection |
Química Nova (Online) |
repository.name.fl_str_mv |
Química Nova (Online) - Sociedade Brasileira de Química (SBQ) |
repository.mail.fl_str_mv |
quimicanova@sbq.org.br |
_version_ |
1750318121061711872 |