Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae

Detalhes bibliográficos
Autor(a) principal: Nóbrega, Cláudia S.
Data de Publicação: 2017
Outros Autores: Raposo, Mariana, Van Driessche, Gonzalez, Devreese, Bart, 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/10362/134168
Resumo: Fundacao para a Ciencia e a Tecnologia - PTDC/BIA-PRO/109796/2009 ; SFRH/BD/87878/2012 ; FCT/MEC - UID/Multi/04378/2013; ERDF - POCI-01-0145-FEDER-007728; Belgian Federal Science Policy Office (Belspo) - IAP7/44
id RCAP_b423daf5cebab83bd183f1969ed7dce9
oai_identifier_str oai:run.unl.pt:10362/134168
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeaeBacterial peroxidaseHeme enzymeKineticsNeisseria gonorrhoeaeReactive oxygen speciesBiochemistryInorganic ChemistryFundacao para a Ciencia e a Tecnologia - PTDC/BIA-PRO/109796/2009 ; SFRH/BD/87878/2012 ; FCT/MEC - UID/Multi/04378/2013; ERDF - POCI-01-0145-FEDER-007728; Belgian Federal Science Policy Office (Belspo) - IAP7/44Neisseria gonorrhoeae is an obligate human pathogen that expresses an array of molecular systems to detoxify reactive oxygen species as defense mechanisms during colonization and infection. One of these is the bacterial peroxidase that reduces H2O2 to water in its periplasm. The soluble form of this enzyme was heterologously expressed in E. coli in the holo-form binding two c-types hemes, a high-potential E heme and a low-potential P heme, with redox potentials of (+ 310 mV) and (− 190 mV/− 300 mV), respectively in the presence of calcium ions, at pH 7.5. Visible and EPR spectroscopic analysis together with activity assays indicate the presence of a calcium dependent reductive activation mechanism in thgonorrhoeaeNeisseria gonorrhoeae bacterial peroxidase, in which P heme is bis-His coordinated low-spin in the fully oxidized state of the enzyme, and becomes penta-coordinated high-spin upon reduction of E heme in the presence of calcium ions. The activated enzyme has a high affinity for H2O2 (KM of 4 ± 1 μM), with maximum activity being attained at pH 7.0 and 37 °C, with the rate-limiting step in the catalytic cycle being the electron transfer between the two hemes. In this enzyme, dimer formation is not promoted at high ionic strength, thus differing from the classical bacterial peroxidases. These results contribute to the understanding of the involvement of Neisseria gonorrhoeae bacterial peroxidase has a first line defense mechanism against exogenously produced hydrogen peroxide in the host environment.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNNóbrega, Cláudia S.Raposo, MarianaVan Driessche, GonzalezDevreese, BartPauleta, Sofia R.2022-03-09T23:18:34Z2017-06-012017-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article12application/pdfhttp://hdl.handle.net/10362/134168eng0162-0134PURE: 2517305https://doi.org/10.1016/j.jinorgbio.2017.03.007info: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:RCAAP2024-03-11T05:12:36Zoai:run.unl.pt:10362/134168Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:48:00.230154Repositório 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 Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
title Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
spellingShingle Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
Nóbrega, Cláudia S.
Bacterial peroxidase
Heme enzyme
Kinetics
Neisseria gonorrhoeae
Reactive oxygen species
Biochemistry
Inorganic Chemistry
title_short Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
title_full Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
title_fullStr Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
title_full_unstemmed Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
title_sort Biochemical characterization of the bacterial peroxidase from the human pathogen Neisseria gonorrhoeae
author Nóbrega, Cláudia S.
author_facet Nóbrega, Cláudia S.
Raposo, Mariana
Van Driessche, Gonzalez
Devreese, Bart
Pauleta, Sofia R.
author_role author
author2 Raposo, Mariana
Van Driessche, Gonzalez
Devreese, Bart
Pauleta, Sofia R.
author2_role author
author
author
author
dc.contributor.none.fl_str_mv UCIBIO - Applied Molecular Biosciences Unit
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Nóbrega, Cláudia S.
Raposo, Mariana
Van Driessche, Gonzalez
Devreese, Bart
Pauleta, Sofia R.
dc.subject.por.fl_str_mv Bacterial peroxidase
Heme enzyme
Kinetics
Neisseria gonorrhoeae
Reactive oxygen species
Biochemistry
Inorganic Chemistry
topic Bacterial peroxidase
Heme enzyme
Kinetics
Neisseria gonorrhoeae
Reactive oxygen species
Biochemistry
Inorganic Chemistry
description Fundacao para a Ciencia e a Tecnologia - PTDC/BIA-PRO/109796/2009 ; SFRH/BD/87878/2012 ; FCT/MEC - UID/Multi/04378/2013; ERDF - POCI-01-0145-FEDER-007728; Belgian Federal Science Policy Office (Belspo) - IAP7/44
publishDate 2017
dc.date.none.fl_str_mv 2017-06-01
2017-06-01T00:00:00Z
2022-03-09T23:18:34Z
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/10362/134168
url http://hdl.handle.net/10362/134168
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0162-0134
PURE: 2517305
https://doi.org/10.1016/j.jinorgbio.2017.03.007
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 12
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_ 1799138081600700416

Registros relacionados