Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin

Detalhes bibliográficos
Autor(a) principal: Nóbrega, Cláudia S.
Data de Publicação: 2018
Outros Autores: 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/10362/111952
Resumo: cofinanced by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
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spelling Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurinbacterial cytochrome c peroxidaseelectron transfer pathwaylipid-modified azurinmolecular dockingNeisseria gonorrhoeaeprotein–protein interactionBiophysicsStructural BiologyBiochemistryMolecular BiologyGeneticsCell Biologycofinanced by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).The Neisseria gonorrhoeae bacterial cytochrome c peroxidase plays a key role in detoxifying the cells from H2O2 by reducing it to water using the lipid-modified azurin, LAz, a small type 1 copper protein, as electron donor. Here, the interaction between these two proteins was characterized by steady-state kinetics, two-dimensional NMR and molecular docking simulations. LAz is an efficient electron donor capable of activating this enzyme. This electron transfer complex is weak with a hydrophobic character, with LAz binding close to the electron transferring heme of the enzyme. The high catalytic rate (39 ± 0.03 s−1) is explained by the LAz pre-orientation, due to a positive dipole moment, and by the fast-dynamic ensemble of orientations, suggested by the small chemical shifts.UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNNóbrega, Cláudia S.Pauleta, Sofia R.2021-02-16T23:19:20Z2018-05-012018-05-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article11application/pdfhttp://hdl.handle.net/10362/111952eng0014-5793PURE: 4409266https://doi.org/10.1002/1873-3468.13053info: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:RCAAP2024-03-11T04:55:41Zoai:run.unl.pt:10362/111952Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:42:01.791232Repositório 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 Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
title Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
spellingShingle Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
Nóbrega, Cláudia S.
bacterial cytochrome c peroxidase
electron transfer pathway
lipid-modified azurin
molecular docking
Neisseria gonorrhoeae
protein–protein interaction
Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology
title_short Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
title_full Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
title_fullStr Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
title_full_unstemmed Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
title_sort Interaction between Neisseria gonorrhoeae bacterial peroxidase and its electron donor, the lipid-modified azurin
author Nóbrega, Cláudia S.
author_facet Nóbrega, Cláudia S.
Pauleta, Sofia R.
author_role author
author2 Pauleta, Sofia R.
author2_role 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.
Pauleta, Sofia R.
dc.subject.por.fl_str_mv bacterial cytochrome c peroxidase
electron transfer pathway
lipid-modified azurin
molecular docking
Neisseria gonorrhoeae
protein–protein interaction
Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology
topic bacterial cytochrome c peroxidase
electron transfer pathway
lipid-modified azurin
molecular docking
Neisseria gonorrhoeae
protein–protein interaction
Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology
description cofinanced by the ERDF under the PT2020 Partnership Agreement (POCI-01-0145-FEDER-007728).
publishDate 2018
dc.date.none.fl_str_mv 2018-05-01
2018-05-01T00:00:00Z
2021-02-16T23:19:20Z
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/10362/111952
url http://hdl.handle.net/10362/111952
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0014-5793
PURE: 4409266
https://doi.org/10.1002/1873-3468.13053
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 11
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
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