Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study

Bibliographic Details
Main Author: Pedroso, Humberto A.
Publication Date: 2016
Other Authors: Silveira, Célia M., Almeida, Rui M., Almeida, Ana, Besson, Stéphane, Moura, Isabel, Moura, José J G, Almeida, Maria Gabriela Machado de
Format: Article
Language: eng
Source: Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
Download full: https://doi.org/10.1016/j.bbabio.2016.04.279
Summary: The authors acknowledge funding from UCIBIO@REQUIMTE Pest-C/EQB/LA0006/2013. CM Silveira and RM Almeida thank the financial support from Fundacao para a Ciencia e Tecnologia (Postdoctoral fellowships SFRH/BPD/79566/2011 and SFRH/BPD/80293/2011).
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spelling Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative studyCytochrome cCytochrome cd nitrite reductaseElectronic pathwaysIntermolecular electron transferMediated electrochemistryMolecular couplingBiophysicsBiochemistryCell BiologyThe authors acknowledge funding from UCIBIO@REQUIMTE Pest-C/EQB/LA0006/2013. CM Silveira and RM Almeida thank the financial support from Fundacao para a Ciencia e Tecnologia (Postdoctoral fellowships SFRH/BPD/79566/2011 and SFRH/BPD/80293/2011).Cytochrome cd1 nitrite reductases (cd1NiRs) catalyze the reduction of nitrite to nitric oxide in denitrifying bacteria, such as Marinobacter hydrocarbonoclasticus. Previous work demonstrated that the enzymatic activity depends on a structural pre-activation triggered by the entry of electrons through the electron transfer (ET) domain, which houses a heme c center. The catalytic activity of M. hydrocarbonoclasticus cd1NiR (Mhcd1NiR) was tested by mediated electrochemistry, using small ET proteins and chemical redox mediators. The rate of enzymatic reaction depends on the nature of the redox partner, with cytochrome (cyt) c552 providing the highest value. In situations where cyt c552 is replaced by either a biological (cyt c from horse heart) or a chemical mediator the catalytic response was only observed at very low scan rates, suggesting that the intermolecular ET rate is much slower. Molecular docking simulations with the 3D model structure of Mhcd1NiR and cyt c552 or cyt c showed that hydrophobic interactions favor the formation of complexes where the heme c domain of the enzyme is the principal docking site. However, only in the case of cyt c552 the preferential areas of contact and Fe-Fe distances between heme c groups of the redox partners allow establishing competent ET pathways. The coupling of the enzyme with chemical redox mediators was also found not to be energetically favorable. These results indicate that although low activity functional complexes can be formed between Mhcd1NiR and different types of redox mediators, efficient ET is only observed with the putative physiological electron donor cyt c552.Molecular, Structural and Cellular Microbiology (MOSTMICRO)Instituto de Tecnologia Química e Biológica António Xavier (ITQB)UCIBIO - Applied Molecular Biosciences UnitDQ - Departamento de QuímicaRUNPedroso, Humberto A.Silveira, Célia M.Almeida, Rui M.Almeida, AnaBesson, StéphaneMoura, IsabelMoura, José J GAlmeida, Maria Gabriela Machado de2018-05-02T22:05:15Z2016-09-012016-09-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article10application/pdfhttps://doi.org/10.1016/j.bbabio.2016.04.279eng0005-2728PURE: 1954570http://www.scopus.com/inward/record.url?scp=84974603879&partnerID=8YFLogxKhttps://doi.org/10.1016/j.bbabio.2016.04.279info:eu-repo/semantics/openAccessreponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiainstacron:RCAAP2024-05-22T17:32:16Zoai:run.unl.pt:10362/35836Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireinfo@rcaap.ptopendoar:https://opendoar.ac.uk/repository/71602025-05-28T17:03:20.223676Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologiafalse
dc.title.none.fl_str_mv Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
title Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
spellingShingle Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
Pedroso, Humberto A.
Cytochrome c
Cytochrome cd nitrite reductase
Electronic pathways
Intermolecular electron transfer
Mediated electrochemistry
Molecular coupling
Biophysics
Biochemistry
Cell Biology
title_short Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
title_full Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
title_fullStr Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
title_full_unstemmed Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
title_sort Electron transfer and docking between cytochrome cd1 nitrite reductase and different redox partners - A comparative study
author Pedroso, Humberto A.
author_facet Pedroso, Humberto A.
Silveira, Célia M.
Almeida, Rui M.
Almeida, Ana
Besson, Stéphane
Moura, Isabel
Moura, José J G
Almeida, Maria Gabriela Machado de
author_role author
author2 Silveira, Célia M.
Almeida, Rui M.
Almeida, Ana
Besson, Stéphane
Moura, Isabel
Moura, José J G
Almeida, Maria Gabriela Machado de
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Molecular, Structural and Cellular Microbiology (MOSTMICRO)
Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
UCIBIO - Applied Molecular Biosciences Unit
DQ - Departamento de Química
RUN
dc.contributor.author.fl_str_mv Pedroso, Humberto A.
Silveira, Célia M.
Almeida, Rui M.
Almeida, Ana
Besson, Stéphane
Moura, Isabel
Moura, José J G
Almeida, Maria Gabriela Machado de
dc.subject.por.fl_str_mv Cytochrome c
Cytochrome cd nitrite reductase
Electronic pathways
Intermolecular electron transfer
Mediated electrochemistry
Molecular coupling
Biophysics
Biochemistry
Cell Biology
topic Cytochrome c
Cytochrome cd nitrite reductase
Electronic pathways
Intermolecular electron transfer
Mediated electrochemistry
Molecular coupling
Biophysics
Biochemistry
Cell Biology
description The authors acknowledge funding from UCIBIO@REQUIMTE Pest-C/EQB/LA0006/2013. CM Silveira and RM Almeida thank the financial support from Fundacao para a Ciencia e Tecnologia (Postdoctoral fellowships SFRH/BPD/79566/2011 and SFRH/BPD/80293/2011).
publishDate 2016
dc.date.none.fl_str_mv 2016-09-01
2016-09-01T00:00:00Z
2018-05-02T22:05:15Z
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 https://doi.org/10.1016/j.bbabio.2016.04.279
url https://doi.org/10.1016/j.bbabio.2016.04.279
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 0005-2728
PURE: 1954570
http://www.scopus.com/inward/record.url?scp=84974603879&partnerID=8YFLogxK
https://doi.org/10.1016/j.bbabio.2016.04.279
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv 10
application/pdf
dc.source.none.fl_str_mv reponame:Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
instname:FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron:RCAAP
instname_str FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
instacron_str RCAAP
institution RCAAP
reponame_str Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
collection Repositórios Científicos de Acesso Aberto de Portugal (RCAAP)
repository.name.fl_str_mv Repositórios Científicos de Acesso Aberto de Portugal (RCAAP) - FCCN, serviços digitais da FCT – Fundação para a Ciência e a Tecnologia
repository.mail.fl_str_mv info@rcaap.pt
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