{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T03:23:26Z","timestamp":1791429806913,"version":"4.3.3"},"reference-count":71,"publisher":"MDPI AG","issue":"6","license":[{"start":{"date-parts":[[2018,5,26]],"date-time":"2018-05-26T00:00:00Z","timestamp":1527292800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["R01GM101225"],"award-info":[{"award-number":["R01GM101225"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>We examine the effect of oxidative stress on the stability of mitochondrial respiratory complexes and their association into supercomplexes (SCs) in the neuron-specific Rieske iron sulfur protein (RISP) and COX10 knockout (KO) mice. Previously we reported that these two models display different grades of oxidative stress in distinct brain regions. Using blue native gel electrophoresis, we observed a redistribution of the architecture of SCs in KO mice. Brain regions with moderate levels of oxidative stress (cingulate cortex of both COX10 and RISP KO and hippocampus of the RISP KO) showed a significant increase in the levels of high molecular weight (HMW) SCs. High levels of oxidative stress in the piriform cortex of the RISP KO negatively impacted the stability of CI, CIII and SCs. Treatment of the RISP KO with the mitochondrial targeted antioxidant mitoTEMPO preserved the stability of respiratory complexes and formation of SCs in the piriform cortex and increased the levels of glutathione peroxidase. These results suggest that mild to moderate levels of oxidative stress can modulate SCs into a more favorable architecture of HMW SCs to cope with rising levels of free radicals and cover the energetic needs.<\/jats:p>","DOI":"10.3390\/ijms19061582","type":"journal-article","created":{"date-parts":[[2018,5,29]],"date-time":"2018-05-29T02:58:18Z","timestamp":1527562698000},"page":"1582","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["The Organization of Mitochondrial Supercomplexes is Modulated by Oxidative Stress In Vivo in Mouse Models of Mitochondrial Encephalopathy"],"prefix":"10.3390","volume":"19","author":[{"given":"Mir R.","family":"Anwar","sequence":"first","affiliation":[{"name":"Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amy","family":"Saldana-Caboverde","sequence":"additional","affiliation":[{"name":"Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sofia","family":"Garcia","sequence":"additional","affiliation":[{"name":"Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1252-0594","authenticated-orcid":false,"given":"Francisca","family":"Diaz","sequence":"additional","affiliation":[{"name":"Department of Neurology, University of Miami Miller School of Medicine, Miami, FL 33136, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2018,5,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"306","DOI":"10.1016\/j.freeradbiomed.2009.11.001","article-title":"Nitration of the mitochondrial complex I subunit NDUFB8 elicits RIP1- and RIP3-mediated necrosis","volume":"48","author":"Davis","year":"2010","journal-title":"Free Radic. Biol. Med."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"39646","DOI":"10.1074\/jbc.M110.164160","article-title":"Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates","volume":"285","author":"Garcia","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/j.semcdb.2017.07.021","article-title":"Respiratory chain supercomplexes: Structures, function and biogenesis","volume":"76","author":"Ugalde","year":"2018","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.bbabio.2008.10.010","article-title":"Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato","volume":"1787","author":"Bultema","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"3379","DOI":"10.1002\/pmic.201000343","article-title":"Large pore gels to separate mega protein complexes larger than 10MDa by blue native electrophoresis: Isolation of putative respiratory strings or patches","volume":"10","author":"Strecker","year":"2010","journal-title":"Proteomics"},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1016\/j.bbabio.2006.05.006","article-title":"Supercomplexes and subcomplexes of mitochondrial oxidative phosphorylation","volume":"1757","author":"Wittig","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1016\/j.molcel.2008.10.021","article-title":"Respiratory Active Mitochondrial Supercomplexes","volume":"32","author":"Peleato","year":"2008","journal-title":"Mol. Cell"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"52873","DOI":"10.1074\/jbc.M308366200","article-title":"Cardiolipin stabilizes respiratory chain supercomplexes","volume":"278","author":"Pfeiffer","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1016\/j.cmet.2012.02.006","article-title":"Identification of a protein mediating respiratory supercomplex stability","volume":"15","author":"Chen","year":"2012","journal-title":"Cell Metab."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1363","DOI":"10.1128\/MCB.06369-11","article-title":"Rcf1 and Rcf2, members of the hypoxia-induced gene 1 protein family, are critical components of the mitochondrial cytochrome bc1-cytochrome c oxidase supercomplex","volume":"32","author":"Strogolova","year":"2012","journal-title":"Mol. Cell. Biol."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.cmet.2012.01.016","article-title":"Rcf1 mediates cytochrome oxidase assembly and respirasome formation, revealing heterogeneity of the enzyme complex","volume":"15","author":"Vukotic","year":"2012","journal-title":"Cell Metab."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1567","DOI":"10.1126\/science.1230381","article-title":"Supercomplex assembly determines electron flux in the mitochondrial electron transport chain","volume":"340","author":"Colas","year":"2013","journal-title":"Science"},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1016\/j.cmet.2014.11.005","article-title":"The respiratory chain supercomplex organization is independent of COX7a2l isoforms","volume":"20","author":"Mourier","year":"2014","journal-title":"Cell Metab."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"2387","DOI":"10.1016\/j.celrep.2016.07.081","article-title":"COX7A2L Is a Mitochondrial Complex III Binding Protein that Stabilizes the III2+IV Supercomplex without Affecting Respirasome Formation","volume":"16","author":"Milenkovic","year":"2016","journal-title":"Cell Rep."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"2302","DOI":"10.1128\/MCB.00189-13","article-title":"MCJ\/DnaJC15, an endogenous mitochondrial repressor of the respiratory chain that controls metabolic alterations","volume":"33","author":"Hatle","year":"2013","journal-title":"Mol. Cell. Biol."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1080\/15216540152845957","article-title":"The mitochondrial production of reactive oxygen species: Mechanisms and implications in human pathology","volume":"52","author":"Lenaz","year":"2001","journal-title":"IUBMB Life"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"740","DOI":"10.1016\/j.bbabio.2008.04.007","article-title":"Is supercomplex organization of the respiratory chain required for optimal electron transfer activity?","volume":"1777","author":"Genova","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1002\/biof.5520250103","article-title":"Supercomplex organization of the mitochondrial respiratory chain and the role of the Coenzyme Q pool: Pathophysiological implications","volume":"25","author":"Genova","year":"2005","journal-title":"Biofactors"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/j.bbabio.2013.11.002","article-title":"Functional role of mitochondrial respiratory supercomplexes","volume":"1837","author":"Genova","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"639","DOI":"10.1038\/nature19359","article-title":"The architecture of the mammalian respirasome","volume":"537","author":"Gu","year":"2016","journal-title":"Nature"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/nature19774","article-title":"The architecture of respiratory supercomplexes","volume":"537","author":"Letts","year":"2016","journal-title":"Nature"},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1598","DOI":"10.1016\/j.cell.2016.11.012","article-title":"Structure of Mammalian Respiratory Supercomplex I1III2IV1","volume":"167","author":"Wu","year":"2016","journal-title":"Cell"},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1247","DOI":"10.1016\/j.cell.2017.07.050","article-title":"Architecture of Human Mitochondrial Respiratory Megacomplex I2III2IV2","volume":"170","author":"Guo","year":"2017","journal-title":"Cell"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1146\/annurev-physiol-021115-105031","article-title":"Supramolecular Organization of Respiratory Complexes","volume":"78","author":"Enriquez","year":"2016","journal-title":"Annu. Rev. Physiol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"800","DOI":"10.1038\/nsmb.3460","article-title":"Clarifying the supercomplex: The higher-order organization of the mitochondrial electron transport chain","volume":"24","author":"Letts","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"765","DOI":"10.1016\/j.cmet.2017.03.009","article-title":"The Enigma of the Respiratory Chain Supercomplex","volume":"25","author":"Milenkovic","year":"2017","journal-title":"Cell Metab."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/j.exger.2010.02.003","article-title":"Ageing alters the supramolecular architecture of OxPhos complexes in rat brain cortex","volume":"45","author":"Frenzel","year":"2010","journal-title":"Exp. Gerontol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"708","DOI":"10.1016\/j.jprot.2009.02.007","article-title":"Defining the transcriptomic and proteomic profiles of rat ageing skeletal muscle by the use of a cDNA array, 2D- and Blue native-PAGE approach","volume":"72","author":"Lombardi","year":"2009","journal-title":"J. Proteom."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1093\/cvr\/cvn184","article-title":"Cardiac mitochondria in heart failure: Decrease in respirasomes and oxidative phosphorylation","volume":"80","author":"Rosca","year":"2008","journal-title":"Cardiovasc. Res."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1016\/j.neuint.2017.03.023","article-title":"Mitochondrial respiratory chain disorganization in Parkinson's disease-relevant PINK1 and DJ1 mutants","volume":"109","author":"Azkona","year":"2017","journal-title":"Neurochem. Int."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"301","DOI":"10.1016\/j.cmet.2016.11.004","article-title":"Enhanced Respiratory Chain Supercomplex Formation in Response to Exercise in Human Skeletal Muscle","volume":"25","author":"Greggio","year":"2017","journal-title":"Cell Metab."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"3247","DOI":"10.1091\/mbc.e10-01-0025","article-title":"Hypoxia-inducible factor-1 activation in nonhypoxic conditions: The essential role of mitochondrial-derived reactive oxygen species","volume":"21","author":"Patten","year":"2010","journal-title":"Mol. Biol. Cell"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"364","DOI":"10.1016\/S0014-5793(01)02850-2","article-title":"The site of production of superoxide radical in mitochondrial Complex I is not a bound ubisemiquinone but presumably iron-sulfur cluster N2","volume":"505","author":"Genova","year":"2001","journal-title":"FEBS Lett."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"12697","DOI":"10.1038\/srep12697","article-title":"RCF1-dependent respiratory supercomplexes are integral for lifespan-maintenance in a fungal ageing model","volume":"5","author":"Fischer","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"33972","DOI":"10.1074\/jbc.273.51.33972","article-title":"Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria","volume":"273","author":"Zhang","year":"1998","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1111\/j.1463-1326.2010.01267.x","article-title":"Impact of nitric oxide on metabolism in health and age-related disease","volume":"12","author":"Knott","year":"2010","journal-title":"Diabetes Obes. Metab."},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1016\/j.biocel.2006.07.001","article-title":"Free radicals and antioxidants in normal physiological functions and human disease","volume":"39","author":"Valko","year":"2007","journal-title":"Int. J. Biochem. Cell Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"19603","DOI":"10.1074\/jbc.M209359200","article-title":"Reversible glutathionylation of complex I increases mitochondrial superoxide formation","volume":"278","author":"Taylor","year":"2003","journal-title":"J. Biol. Chem."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1128\/MCB.06051-11","article-title":"Cells lacking Rieske iron-sulfur protein have a reactive oxygen species-associated decrease in respiratory complexes I and IV","volume":"32","author":"Diaz","year":"2012","journal-title":"Mol. Cell. Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"4872","DOI":"10.1128\/MCB.01767-05","article-title":"Cytochrome c oxidase is required for the assembly\/stability of respiratory complex I in mouse fibroblasts","volume":"26","author":"Diaz","year":"2006","journal-title":"Mol. Cell. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.celrep.2016.03.009","article-title":"The CoQH2\/CoQ Ratio Serves as a Sensor of Respiratory Chain Efficiency","volume":"15","author":"Guaras","year":"2016","journal-title":"Cell Rep."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"5066","DOI":"10.1093\/hmg\/dds350","article-title":"A defect in the mitochondrial complex III, but not complex IV, triggers early ROS-dependent damage in defined brain regions","volume":"21","author":"Diaz","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"13063","DOI":"10.1073\/pnas.1613701113","article-title":"Complex I assembly into supercomplexes determines differential mitochondrial ROS production in neurons and astrocytes","volume":"113","author":"Logan","year":"2016","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Francischetti, I.M., Gordon, E., Bizzarro, B., Gera, N., Andrade, B.B., Oliveira, F., Ma, D., Assumpcao, T.C., Ribeiro, J.M., and Pena, M. (2014). Tempol, an intracellular antioxidant, inhibits tissue factor expression, attenuates dendritic cell function, and is partially protective in a murine model of cerebral malaria. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0087140"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1016\/j.bbabio.2013.12.009","article-title":"The function of the respiratory supercomplexes: The plasticity model","volume":"1837","author":"Enriquez","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"36349","DOI":"10.1074\/jbc.M404033200","article-title":"Significance of Respirasomes for the Assembly\/Stability of Human Respiratory Chain Complex I","volume":"279","author":"Schagger","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/S1097-2765(04)00124-8","article-title":"Respiratory Complex III Is Required to Maintain Complex I in Mammalian Mitochondria","volume":"13","author":"Bruno","year":"2004","journal-title":"Mol. Cell"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2157","DOI":"10.1093\/hmg\/ddl141","article-title":"Respiratory chain supercomplexes set the threshold for respiration defects in human mtDNA mutant cybrids","volume":"15","author":"Gajewski","year":"2006","journal-title":"Hum. Mol. Genet."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1152\/physrev.00044.2005","article-title":"The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology","volume":"87","author":"Bedard","year":"2007","journal-title":"Physiol. Rev."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.cmet.2012.01.015","article-title":"Mitochondrial complex I plays an essential role in human respirasome assembly","volume":"15","author":"Fontanesi","year":"2012","journal-title":"Cell Metab."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.cmet.2016.09.002","article-title":"The Assembly Pathway of Mitochondrial Respiratory Chain Complex I","volume":"25","author":"Baertling","year":"2017","journal-title":"Cell Metab."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1016\/j.bbabio.2016.03.031","article-title":"Unraveling the complexity of mitochondrial complex I assembly: A dynamic process","volume":"1857","author":"Nijtmans","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1146\/annurev.biochem.75.103004.142539","article-title":"Energy converting NADH: quinone oxidoreductase (complex I)","volume":"75","author":"Brandt","year":"2006","journal-title":"Annu. Rev. Biochem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1146\/annurev-biochem-070511-103700","article-title":"Mitochondrial complex I","volume":"82","author":"Hirst","year":"2013","journal-title":"Annu. Rev. Biochem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1038\/nrm3997","article-title":"A giant molecular proton pump: Structure and mechanism of respiratory complex I","volume":"16","author":"Sazanov","year":"2015","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1038\/nature19754","article-title":"Accessory subunits are integral for assembly and function of human mitochondrial complex I","volume":"538","author":"Stroud","year":"2016","journal-title":"Nature"},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1016\/j.bbabio.2007.07.008","article-title":"Human mitochondrial complex I assembly: A dynamic and versatile process","volume":"1767","author":"Vogel","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_58","first-page":"134","article-title":"Nuclear gene mutations as the cause of mitochondrial complex III deficiency","volume":"6","author":"Zeviani","year":"2015","journal-title":"Front. Genet."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.bbabio.2011.11.009","article-title":"Biogenesis of the cytochrome bc(1) complex and role of assembly factors","volume":"1817","author":"Smith","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1016\/j.bbabio.2012.11.003","article-title":"LYRM7\/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial Complex III assembly in human cells","volume":"1827","author":"Sanchez","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1111\/j.1742-4658.2009.06916.x","article-title":"Evidence that the assembly of the yeast cytochrome bc1 complex involves the formation of a large core structure in the inner mitochondrial membrane","volume":"276","author":"Zara","year":"2009","journal-title":"FEBS J."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1111\/j.1582-4934.2011.01258.x","article-title":"Why is the partial oxygen pressure of human tissues a crucial parameter? Small molecules and hypoxia","volume":"15","author":"Carreau","year":"2011","journal-title":"J. Cell. Mol. Med."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"1469","DOI":"10.1089\/ars.2012.4845","article-title":"Mitochondrial respiratory supercomplex association limits production of reactive oxygen species from complex I","volume":"19","author":"Maranzana","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"2141","DOI":"10.1093\/hmg\/ddt067","article-title":"The cytochrome b p.278Y>C mutation causative of a multisystem disorder enhances superoxide production and alters supramolecular interactions of respiratory chain complexes","volume":"22","author":"Ghelli","year":"2013","journal-title":"Hum. Mol. Genet."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1016\/j.bbadis.2016.01.007","article-title":"Tissue- and species-specific differences in cytochrome c oxidase assembly induced by SURF1 defects","volume":"1862","author":"Kovarova","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/gbb.12101","article-title":"Genetic variability of respiratory complex abundance, organization and activity in mouse brain","volume":"13","author":"Buck","year":"2014","journal-title":"Genes Brain Behav."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"aad0189","DOI":"10.1126\/science.aad0189","article-title":"Systems proteomics of liver mitochondria function","volume":"352","author":"Williams","year":"2016","journal-title":"Science"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"1406","DOI":"10.1016\/j.freeradbiomed.2007.12.036","article-title":"A mitochondria-targeted nitroxide is reduced to its hydroxylamine by ubiquinol in mitochondria","volume":"44","author":"Trnka","year":"2008","journal-title":"Free Radic. Biol. Med."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"1132","DOI":"10.1111\/acel.12144","article-title":"Novel interactions between mitochondrial superoxide dismutases and the electron transport chain","volume":"12","author":"Suthammarak","year":"2013","journal-title":"Aging Cell"},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1007\/978-1-61779-328-8_20","article-title":"Isolation and functional assessment of mitochondria from small amounts of mouse brain tissue","volume":"793","author":"Chinopoulos","year":"2011","journal-title":"Methods Mol. Biol."},{"key":"ref_71","doi-asserted-by":"crossref","unstructured":"Diaz, F., Barrientos, A., and Fontanesi, F. (2009). Evaluation of the mitochondrial respiratory chain and oxidative phosphorylation system using blue native gel electrophoresis. Curr. Protoc. Hum. Genet.","DOI":"10.1002\/0471142905.hg1904s63"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/19\/6\/1582\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T15:06:04Z","timestamp":1760195164000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/19\/6\/1582"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,5,26]]},"references-count":71,"journal-issue":{"issue":"6","published-online":{"date-parts":[[2018,6]]}},"alternative-id":["ijms19061582"],"URL":"https:\/\/doi.org\/10.3390\/ijms19061582","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,5,26]]}}}