Bacterial peroxidases

Detalhes bibliográficos
Autor(a) principal: Barreiro, Daniela S.
Data de Publicação: 2023
Outros Autores: Oliveira, Ricardo N. S., Pauleta, Sofia R.
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
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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
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url http://hdl.handle.net/10362/151541
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PURE: 56961308
https://doi.org/10.1016/j.ccr.2023.215114
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