YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity

Detalhes bibliográficos
Autor(a) principal: Nóbrega, Cláudia S.
Data de Publicação: 2018
Outros Autores: 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/10362/111951
Resumo: Belgian Federal Science Policy Office (Belspo) (grant to BD, IAP7/44, iPROS project). co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
id RCAP_f0dd080dac02cae986eb46ae9a2637ff
oai_identifier_str oai:run.unl.pt:10362/111951
network_acronym_str RCAP
network_name_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository_id_str 7160
spelling YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activityEscherichia coliHeme enzymeOxidative stressQuinol peroxidase activityTrihemic bacterial peroxidaseBiophysicsBiochemistryCell BiologyBelgian Federal Science Policy Office (Belspo) (grant to BD, IAP7/44, iPROS project). co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).The trihemic bacterial cytochrome c peroxidase from Escherichia coli, YhjA, is a membrane-anchored protein with a C-terminal domain homologous to the classical bacterial peroxidases and an additional N-terminal (NT) heme binding domain. Recombinant YhjA is a 50 kDa monomer in solution with three c-type hemes covalently bound. Here is reported the first biochemical and spectroscopic characterization of YhjA and of the NT domain demonstrating that NT heme is His63/Met125 coordinated. The reduction potentials of P (active site), NT and E hemes were established to be −170 mV, +133 mV and +210 mV, respectively, at pH 7.5. YhjA has quinol peroxidase activity in vitro with optimum activity at pH 7.0 and millimolar range KM values using hydroquinone and menadiol (a menaquinol analogue) as electron donors (KM = 0.6 ± 0.2 and 1.8 ± 0.5 mM H2O2, respectively), with similar turnover numbers (kcat = 19 ± 2 and 13 ± 2 s−1, respectively). YhjA does not require reductive activation for maximum activity, in opposition to classical bacterial peroxidases, as P heme is always high-spin 6-coordinated with a water-derived molecule as distal axial ligand but shares the need for the presence of calcium ions in the kinetic assays. Formation of a ferryl Fe(IV) = O species was observed upon incubation of fully oxidized YhjA with H2O2. The data reported improve our understanding of the biochemical properties and catalytic mechanism of YhjA, a three-heme peroxidase that uses the quinol pool to defend the cells against hydrogen peroxide during transient exposure to oxygenated environments.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNNóbrega, Cláudia S.Devreese, BartPauleta, Sofia R.2021-02-16T23:18:29Z2018-062018-06-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article12application/pdfhttp://hdl.handle.net/10362/111951eng0005-2728PURE: 3879091https://doi.org/10.1016/j.bbabio.2018.03.008info: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:RCAAP2024-05-22T17:50:35Zoai:run.unl.pt:10362/111951Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-05-22T17:50:35Repositório 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 YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
title YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
spellingShingle YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
Nóbrega, Cláudia S.
Escherichia coli
Heme enzyme
Oxidative stress
Quinol peroxidase activity
Trihemic bacterial peroxidase
Biophysics
Biochemistry
Cell Biology
title_short YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
title_full YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
title_fullStr YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
title_full_unstemmed YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
title_sort YhjA - An Escherichia coli trihemic enzyme with quinol peroxidase activity
author Nóbrega, Cláudia S.
author_facet Nóbrega, Cláudia S.
Devreese, Bart
Pauleta, Sofia R.
author_role author
author2 Devreese, Bart
Pauleta, Sofia R.
author2_role 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.
Devreese, Bart
Pauleta, Sofia R.
dc.subject.por.fl_str_mv Escherichia coli
Heme enzyme
Oxidative stress
Quinol peroxidase activity
Trihemic bacterial peroxidase
Biophysics
Biochemistry
Cell Biology
topic Escherichia coli
Heme enzyme
Oxidative stress
Quinol peroxidase activity
Trihemic bacterial peroxidase
Biophysics
Biochemistry
Cell Biology
description Belgian Federal Science Policy Office (Belspo) (grant to BD, IAP7/44, iPROS project). co-financed by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
publishDate 2018
dc.date.none.fl_str_mv 2018-06
2018-06-01T00:00:00Z
2021-02-16T23:18:29Z
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/10362/111951
url http://hdl.handle.net/10362/111951
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0005-2728
PURE: 3879091
https://doi.org/10.1016/j.bbabio.2018.03.008
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 mluisa.alvim@gmail.com
_version_ 1817545780987166720

Registros relacionados