Publication:
Alternative respiratory oxidases to study the animal electron transport chain.

dc.contributor.authorHernansanz-Agustín, Pablo
dc.contributor.authorEnríquez, José Antonio
dc.contributor.funderMinisterio de Economía y Competitividad (España)
dc.contributor.funderInstituto de Salud Carlos III
dc.contributor.funderMinisterio de Ciencia, Innovación y Universidades (España)
dc.contributor.funderFundación ProCNIC
dc.contributor.funderMinisterio de Ciencia e Innovación. Centro de Excelencia Severo Ochoa (España)
dc.contributor.funderUnión Europea. Fondo Europeo de Desarrollo Regional (FEDER/ERDF)
dc.date.accessioned2024-12-04T10:54:20Z
dc.date.available2024-12-04T10:54:20Z
dc.date.issued2023-01-01
dc.descriptionThis study was supported by MINECO: SAF2015-65633-R, RTI2018-099357-B-I00, HFSP (RGP0016/2018) and CIBER (CB16/10/00282) to JAE. The CNIC is supported by the Instituto de Salud Carlos III (ISCIII), the Ministerio de Ciencia, Innovacion ´ y Universidades (MCNU) and the Pro CNIC Foundation and is a Severo Ochoa Center of Excellence (SEV2015-0505). This research has been financed by Spanish Government grants (ISCIII and AEI agencies, partially funded by the European Union FEDER/ERDF). PH-A is recipient of a Juan de la Cierva fellowship (IJC2020-042679-I).
dc.description.abstractOxidative phosphorylation is a common process to most organisms in which the main function is to generate an electrochemical gradient across the inner mitochondrial membrane (IMM) and to make energy available to the cell. However, plants, many fungi and some animals maintain non-energy conserving oxidases which serve as a bypass to coupled respiration. Namely, the alternative NADH:ubiquinone oxidoreductase NDI1, present in the complex I (CI)-lacking Saccharomyces cerevisiae, and the alternative oxidase, ubiquinol:oxygen oxidoreductase AOX, present in many organisms across different kingdoms. In the last few years, these alternative oxidases have been used to dissect previously indivisible processes in bioenergetics and have helped to discover, understand, and corroborate important processes in mitochondria. Here, we review how the use of alternative oxidases have contributed to the knowledge in CI stability, bioenergetics, redox biology, and the implications of their use in current and future research.
dc.description.peerreviewed
dc.format.number1
dc.format.page148936
dc.format.volume1864
dc.identifier.citationBiochim Biophys Acta Bioenerg. 2023 Jan 1;1864(1):148936.
dc.identifier.journalBiochimica et Biophysica Acta. Bioenergetics.
dc.identifier.pubmedID36395975
dc.identifier.urihttps://hdl.handle.net/20.500.12105/25851
dc.language.isoeng
dc.publisherElsevier
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/SAF2015-65633-R
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/RTI2018-099357-B-I00
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/RGP0016/2018
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/CB16/10/00282
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/IJC2020-042679-I
dc.relation.publisherversionhttps://10.1016/j.bbabio.2022.148936
dc.repisalud.institucionCNIC
dc.repisalud.orgCNICCNIC::Grupos de investigación::Genética Funcional del Sistema de Fosforilación Oxidativa
dc.rights.accessRightsopen access
dc.rights.licenseAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectAOX
dc.subjectAlternative oxidase
dc.subjectCoQ pool
dc.subjectOxphos
dc.subjectROS
dc.titleAlternative respiratory oxidases to study the animal electron transport chain.
dc.typeresearch article
dc.type.hasVersionVoR
dspace.entity.typePublication

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