Bacterial peroxidases
Autor(a) principal: | |
---|---|
Data de Publicação: | 2023 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/151541 |
Resumo: | Bacterial peroxidases are responsible for the reduction of hydrogen peroxide to water. Found in the periplasm of gram-negative bacteria, they are one of the defense mechanisms against endogenous and exogenous peroxide stress under low oxygen tensions. Besides being involved in peroxide detoxification, bacterial peroxidases have been proposed to constitute an alternative pathway to the respiratory chain under anoxic conditions, as demonstrated in E. coli that can use hydrogen peroxide as an electron acceptor in the absence of oxygen. Bacterial peroxidases are c-type cytochromes with either two or three c-type hemes bound to the polypeptide chain, being divided into classical or non-classical, respectively. Orthologous to the classical bacterial peroxidases are the MauG enzymes that share some structural, spectroscopic and sequence similarities but have distinct physiological roles (though for most their function remains unknown). The spectroscopic and kinetic data on bacterial peroxidases are reviewed for both classes. Most classical bacterial peroxidases require reductive activation that consists in structural changes so that the catalytic heme becomes accessible to the substrate. However, non-classical enzymes are ready to bind the hydrogen peroxide as their catalytic center is penta-coordinated, which is also observed in their structural model. The few studies that report the involvement of bacterial peroxidases from pathogenic bacteria in biofilms, is an indication that these enzymes might contribute to their infection mechanism and thus can constitute alternative drug targets |
id |
RCAP_d58eca193d0ddfa7d7ce8b8c66d495a1 |
---|---|
oai_identifier_str |
oai:run.unl.pt:10362/151541 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
Bacterial peroxidasesMultivalent enzymes that enable the use of hydrogen peroxide for microaerobic and anaerobic proliferationAgricultural and Biological Sciences(all)Biochemistry, Genetics and Molecular Biology (miscellaneous)SDG 3 - Good Health and Well-beingBacterial peroxidases are responsible for the reduction of hydrogen peroxide to water. Found in the periplasm of gram-negative bacteria, they are one of the defense mechanisms against endogenous and exogenous peroxide stress under low oxygen tensions. Besides being involved in peroxide detoxification, bacterial peroxidases have been proposed to constitute an alternative pathway to the respiratory chain under anoxic conditions, as demonstrated in E. coli that can use hydrogen peroxide as an electron acceptor in the absence of oxygen. Bacterial peroxidases are c-type cytochromes with either two or three c-type hemes bound to the polypeptide chain, being divided into classical or non-classical, respectively. Orthologous to the classical bacterial peroxidases are the MauG enzymes that share some structural, spectroscopic and sequence similarities but have distinct physiological roles (though for most their function remains unknown). The spectroscopic and kinetic data on bacterial peroxidases are reviewed for both classes. Most classical bacterial peroxidases require reductive activation that consists in structural changes so that the catalytic heme becomes accessible to the substrate. However, non-classical enzymes are ready to bind the hydrogen peroxide as their catalytic center is penta-coordinated, which is also observed in their structural model. The few studies that report the involvement of bacterial peroxidases from pathogenic bacteria in biofilms, is an indication that these enzymes might contribute to their infection mechanism and thus can constitute alternative drug targetsDQ - Departamento de QuímicaUCIBIO - Applied Molecular Biosciences UnitRUNBarreiro, Daniela S.Oliveira, Ricardo N. S.Pauleta, Sofia R.2023-04-03T22:14:39Z2023-06-012023-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article18application/pdfhttp://hdl.handle.net/10362/151541eng0010-8545PURE: 56961308https://doi.org/10.1016/j.ccr.2023.215114info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:33:57Zoai:run.unl.pt:10362/151541Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:54:37.527928Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse |
dc.title.none.fl_str_mv |
Bacterial peroxidases Multivalent enzymes that enable the use of hydrogen peroxide for microaerobic and anaerobic proliferation |
title |
Bacterial peroxidases |
spellingShingle |
Bacterial peroxidases Barreiro, Daniela S. Agricultural and Biological Sciences(all) Biochemistry, Genetics and Molecular Biology (miscellaneous) SDG 3 - Good Health and Well-being |
title_short |
Bacterial peroxidases |
title_full |
Bacterial peroxidases |
title_fullStr |
Bacterial peroxidases |
title_full_unstemmed |
Bacterial peroxidases |
title_sort |
Bacterial peroxidases |
author |
Barreiro, Daniela S. |
author_facet |
Barreiro, Daniela S. Oliveira, Ricardo N. S. Pauleta, Sofia R. |
author_role |
author |
author2 |
Oliveira, Ricardo N. S. Pauleta, Sofia R. |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
DQ - Departamento de Química UCIBIO - Applied Molecular Biosciences Unit RUN |
dc.contributor.author.fl_str_mv |
Barreiro, Daniela S. Oliveira, Ricardo N. S. Pauleta, Sofia R. |
dc.subject.por.fl_str_mv |
Agricultural and Biological Sciences(all) Biochemistry, Genetics and Molecular Biology (miscellaneous) SDG 3 - Good Health and Well-being |
topic |
Agricultural and Biological Sciences(all) Biochemistry, Genetics and Molecular Biology (miscellaneous) SDG 3 - Good Health and Well-being |
description |
Bacterial peroxidases are responsible for the reduction of hydrogen peroxide to water. Found in the periplasm of gram-negative bacteria, they are one of the defense mechanisms against endogenous and exogenous peroxide stress under low oxygen tensions. Besides being involved in peroxide detoxification, bacterial peroxidases have been proposed to constitute an alternative pathway to the respiratory chain under anoxic conditions, as demonstrated in E. coli that can use hydrogen peroxide as an electron acceptor in the absence of oxygen. Bacterial peroxidases are c-type cytochromes with either two or three c-type hemes bound to the polypeptide chain, being divided into classical or non-classical, respectively. Orthologous to the classical bacterial peroxidases are the MauG enzymes that share some structural, spectroscopic and sequence similarities but have distinct physiological roles (though for most their function remains unknown). The spectroscopic and kinetic data on bacterial peroxidases are reviewed for both classes. Most classical bacterial peroxidases require reductive activation that consists in structural changes so that the catalytic heme becomes accessible to the substrate. However, non-classical enzymes are ready to bind the hydrogen peroxide as their catalytic center is penta-coordinated, which is also observed in their structural model. The few studies that report the involvement of bacterial peroxidases from pathogenic bacteria in biofilms, is an indication that these enzymes might contribute to their infection mechanism and thus can constitute alternative drug targets |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-04-03T22:14:39Z 2023-06-01 2023-06-01T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/151541 |
url |
http://hdl.handle.net/10362/151541 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0010-8545 PURE: 56961308 https://doi.org/10.1016/j.ccr.2023.215114 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
18 application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação instacron:RCAAP |
instname_str |
Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
instacron_str |
RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
collection |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository.name.fl_str_mv |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
repository.mail.fl_str_mv |
|
_version_ |
1799138134665986048 |