Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV

The proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to cell aging and other related pathologies. Here, we discuss three current views-the so-called solid, fluid and plasticity models-which descri...

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Autores: Pérez Mejías, Gonzalo, Guerra Castellano, Alejandra, Díaz Quintana, Antonio Jesús, Rosa Acosta, Miguel Ángel de la, Díaz Moreno, Irene
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2019
País:España
Institución:Universidad de Sevilla (US)
Repositorio:idUS. Depósito de Investigación de la Universidad de Sevilla
OAI Identifier:oai:idus.us.es:11441/87640
Acceso en línea:https://hdl.handle.net/11441/87640
https://doi.org/10.1016/j.csbj.2019.05.002
Access Level:acceso abierto
Palabra clave:Cytochrome c
Mitochondria
Phosphorylation
Reactive oxygen species
Respiratory supercomplexes
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spelling Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IVPérez Mejías, GonzaloGuerra Castellano, AlejandraDíaz Quintana, Antonio JesúsRosa Acosta, Miguel Ángel de laDíaz Moreno, IreneCytochrome cMitochondriaPhosphorylationReactive oxygen speciesRespiratory supercomplexesThe proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to cell aging and other related pathologies. Here, we discuss three current views-the so-called solid, fluid and plasticity models-which describe the organization of the main membrane-embedded mitochondrial protein complexes and the key elements that regulate and/or facilitate supercomplex assembly. The soluble electron carrier cytochrome c has recently emerged as an essential factor in the assembly and function of respiratory supercomplexes. In fact, a 'restricted diffusion pathway' mechanism for electron transfer between complexes III and IV has been proposed based on the secondary, distal binding sites for cytochrome c at its two membrane partners recently discovered. This channeling pathway facilitates the surfing of cytochrome c on both respiratory complexes, thereby tuning the efficiency of oxidative phosphorylation and diminishing the production of reactive oxygen species. The well-documented post-translational modifications of cytochrome c could further contribute to the rapid adjustment of electron flow in response to changing cellular conditions.Spanish Ministry of Economy and Competitiveness (BFU2015-71017/BMC MINECO/FEDER and PGC2018-096049-B-I00 BIO/BMC MICINN/FEDER, EU)ElsevierBiología Vegetal y Ecología2019info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfapplication/pdfhttps://hdl.handle.net/11441/87640https://doi.org/10.1016/j.csbj.2019.05.002reponame:idUS. Depósito de Investigación de la Universidad de Sevillainstname:Universidad de Sevilla (US)InglésComputational and Structural Biotechnology Journal, 17, 654-660.BFU2015-71017/BMC MINECO/FEDER and PGC2018-096049-B-I00 BIO/BMC MICINN/FEDER, EUhttp://dx.doi.org/10.1016/j.csbj.2019.05.002info:eu-repo/semantics/openAccessoai:idus.us.es:11441/876402026-06-17T12:51:07Z
dc.title.none.fl_str_mv Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
title Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
spellingShingle Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
Pérez Mejías, Gonzalo
Cytochrome c
Mitochondria
Phosphorylation
Reactive oxygen species
Respiratory supercomplexes
title_short Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
title_full Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
title_fullStr Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
title_full_unstemmed Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
title_sort Cytochrome c: Surfing Off of the Mitochondrial Membrane on the Tops of Complexes III and IV
dc.creator.none.fl_str_mv Pérez Mejías, Gonzalo
Guerra Castellano, Alejandra
Díaz Quintana, Antonio Jesús
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
author Pérez Mejías, Gonzalo
author_facet Pérez Mejías, Gonzalo
Guerra Castellano, Alejandra
Díaz Quintana, Antonio Jesús
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
author_role author
author2 Guerra Castellano, Alejandra
Díaz Quintana, Antonio Jesús
Rosa Acosta, Miguel Ángel de la
Díaz Moreno, Irene
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Biología Vegetal y Ecología
dc.subject.none.fl_str_mv Cytochrome c
Mitochondria
Phosphorylation
Reactive oxygen species
Respiratory supercomplexes
topic Cytochrome c
Mitochondria
Phosphorylation
Reactive oxygen species
Respiratory supercomplexes
description The proper arrangement of protein components within the respiratory electron transport chain is nowadays a matter of intense debate, since altering it leads to cell aging and other related pathologies. Here, we discuss three current views-the so-called solid, fluid and plasticity models-which describe the organization of the main membrane-embedded mitochondrial protein complexes and the key elements that regulate and/or facilitate supercomplex assembly. The soluble electron carrier cytochrome c has recently emerged as an essential factor in the assembly and function of respiratory supercomplexes. In fact, a 'restricted diffusion pathway' mechanism for electron transfer between complexes III and IV has been proposed based on the secondary, distal binding sites for cytochrome c at its two membrane partners recently discovered. This channeling pathway facilitates the surfing of cytochrome c on both respiratory complexes, thereby tuning the efficiency of oxidative phosphorylation and diminishing the production of reactive oxygen species. The well-documented post-translational modifications of cytochrome c could further contribute to the rapid adjustment of electron flow in response to changing cellular conditions.
publishDate 2019
dc.date.none.fl_str_mv 2019
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/11441/87640
https://doi.org/10.1016/j.csbj.2019.05.002
url https://hdl.handle.net/11441/87640
https://doi.org/10.1016/j.csbj.2019.05.002
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Computational and Structural Biotechnology Journal, 17, 654-660.
BFU2015-71017/BMC MINECO/FEDER and PGC2018-096049-B-I00 BIO/BMC MICINN/FEDER, EU
http://dx.doi.org/10.1016/j.csbj.2019.05.002
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:idUS. Depósito de Investigación de la Universidad de Sevilla
instname:Universidad de Sevilla (US)
instname_str Universidad de Sevilla (US)
reponame_str idUS. Depósito de Investigación de la Universidad de Sevilla
collection idUS. Depósito de Investigación de la Universidad de Sevilla
repository.name.fl_str_mv
repository.mail.fl_str_mv
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