2025
Polyamine metabolism is dysregulated in COXFA4-related mitochondrial disease
Marquez J, Viviano S, Beckman E, Thies J, Friedland-Little J, Lam C, Deniz E, Shelkowitz E. Polyamine metabolism is dysregulated in COXFA4-related mitochondrial disease. Human Genetics And Genomics Advances 2025, 6: 100418. PMID: 39967265, PMCID: PMC11946867, DOI: 10.1016/j.xhgg.2025.100418.Peer-Reviewed Original ResearchOrnithine decarboxylase pathwayCytochrome c oxidaseMitochondrial diseaseCause of mitochondrial diseaseAnalysis of cellular gene expressionSubunits of cytochrome c oxidaseC oxidaseTissue-specific diseasesCellular gene expressionDeficiency of cytochrome c oxidaseLeigh-like diseaseElectron donor NADHDownstream deficienciesMitochondrial membraneProtein complexesCellular functionsOxidative phosphorylationProtein subunitsGene expressionMetabolic pathwaysPolyamine metabolismPathwayProteinPoor growthAdenosine triphosphate
2018
Insights into the evolution and drug susceptibility of Babesia duncani from the sequence of its mitochondrial and apicoplast genomes
Virji AZ, Thekkiniath J, Ma W, Lawres L, Knight J, Swei A, Roch KL, Mamoun C. Insights into the evolution and drug susceptibility of Babesia duncani from the sequence of its mitochondrial and apicoplast genomes. International Journal For Parasitology 2018, 49: 105-113. PMID: 30176236, PMCID: PMC6395566, DOI: 10.1016/j.ijpara.2018.05.008.Peer-Reviewed Original ResearchConceptsMitochondrial genomeApicoplast genomeB. duncaniCytochrome c oxidaseB. microtiOrganelle proteinsCircular moleculeApicomplexan parasitesPhylogenetic analysisNew lineageGene transcriptionCytochrome bGenomeC oxidaseI proteinPlasmodium sppProteinTheileria sppBabesia bovisKbParasite factorsCausative agentParasitesAnnotationSpp
2013
Functional modulation of mitochondrial cytochrome c oxidase underlies adaptation to high-altitude hypoxia in a Tibetan migratory locust
Zhang ZY, Chen B, Zhao DJ, Kang L. Functional modulation of mitochondrial cytochrome c oxidase underlies adaptation to high-altitude hypoxia in a Tibetan migratory locust. Proceedings Of The Royal Society B 2013, 280: 20122758. PMID: 23390104, PMCID: PMC3574369, DOI: 10.1098/rspb.2012.2758.Peer-Reviewed Original ResearchConceptsCytochrome c oxidaseOxidative phosphorylationLocust populationsHypoxia responseMigratory locustHypoxia toleranceC oxidaseMitochondrial cytochrome c oxidaseElectron transport rateElevated catalytic efficiencyHigher hypoxia toleranceCatalytic redox centerHypoxia adaptationCOX activityMitochondrial structureAerobic organismsFlight musclesMitochondrial mechanismsNovel mechanismLocusta migratoriaLocustFunctional modulationPermanent hypoxiaHypoxic treatmentProtein content
2006
The calcium-sensitive large-conductance potassium channel (BK/MAXI K) is present in the inner mitochondrial membrane of rat brain
Douglas R, Lai J, Bian S, Cummins L, Moczydlowski E, Haddad G. The calcium-sensitive large-conductance potassium channel (BK/MAXI K) is present in the inner mitochondrial membrane of rat brain. Neuroscience 2006, 139: 1249-1261. PMID: 16567053, DOI: 10.1016/j.neuroscience.2006.01.061.Peer-Reviewed Original ResearchConceptsLarge conductance voltageInner mitochondrial membraneCalcium-sensitive channelsCytochrome c oxidaseMitochondrial membraneInner mitochondrial membrane proteinC oxidaseMitochondrial fractionInner membrane 23Mitochondrial-specific proteinsMitochondrial membrane proteinMicrotubule-associated protein 1Endoplasmic reticulum markerImmuno-gold electron microscopyLarge-conductance potassium channelsDiscrete subcellular fractionsGold particle labellingWestern blottingGolgi proteinsMembrane proteinsSubcellular localizationAlpha subunitProtein 1Mitochondrial pelletMitochondria
2005
Mechanistic Comparisons Between Photosystem II and Cytochrome c Oxidase
Brudvig G, Wikström M. Mechanistic Comparisons Between Photosystem II and Cytochrome c Oxidase. Advances In Photosynthesis And Respiration 2005, 22: 697-713. DOI: 10.1007/1-4020-4254-x_32.Peer-Reviewed Original ResearchFour-electron reductionSingle reaction stepSame chemical reactionPhotosystem IIRole of protonsOxygen reductionProton transferMolecular oxygenReaction mechanismReaction stepsActive siteWater reactionChemical reactionsRequirement of electronsMechanistic comparisonReverse reactionReactionCytochrome c oxidaseProtonsC oxidaseMechanistic similaritiesChemistryElectronsWaterRespiratory enzymes
2000
Kinetics and control of oxidative phosphorylation in rat liver mitochondria after chronic ethanol feeding.
Marcinkeviciute A, Mildaziene V, Crumm S, Demin O, Hoek J, Kholodenko B. Kinetics and control of oxidative phosphorylation in rat liver mitochondria after chronic ethanol feeding. Biochemical Journal 2000, 349: 519-26. PMID: 10880351, PMCID: PMC1221175, DOI: 10.1042/0264-6021:3490519.Peer-Reviewed Original ResearchConceptsOxidative phosphorylationRespiratory fluxMitochondrial proton leakRat liver mitochondriaMitochondrial oxidative phosphorylationCytochrome c oxidaseMitochondrial energy metabolismATP synthaseLiver mitochondriaProton leakC oxidaseProtonmotive forceState 3Blocks of reactionsPhosphorylationEnergy metabolismMitochondriaMitochondrial malfunctioningRespiration rateRespiratory activityRespiratory subsystemIndividual functional unitsFunctional unitsKinetics and control of oxidative phosphorylation in rat liver mitochondria after chronic ethanol feeding
MARCINKEVICIUTE A, MILDAZIENE V, CRUMM S, DEMIN O, HOEK J, KHOLODENKO B. Kinetics and control of oxidative phosphorylation in rat liver mitochondria after chronic ethanol feeding. Biochemical Journal 2000, 349: 519-526. DOI: 10.1042/bj3490519.Peer-Reviewed Original ResearchOxidative phosphorylationRespiratory fluxMitochondrial proton leakRat liver mitochondriaMitochondrial oxidative phosphorylationCytochrome c oxidaseMitochondrial energy metabolismATP synthaseLiver mitochondriaBc1 complexProton leakC oxidaseProtonmotive forceState 3PhosphorylationBlocks of reactionsEnergy metabolismMitochondriaMitochondrial malfunctioningRespiration rateRespiratory activityRespiratory subsystemIndividual functional unitsFunctional unitsLow activity
1983
The Structure of the Metal Centers in Cytochrome c Oxidase
Chan S, Martin C, Wang H, Brudvig G, Stevens T. The Structure of the Metal Centers in Cytochrome c Oxidase. Nato Science Series C: 1983, 313-328. DOI: 10.1007/978-94-009-7049-6_27.Peer-Reviewed Original ResearchMetal centerLow-temperature electron paramagnetic resonance (EPR) spectroscopyElectron nuclear double resonance spectroscopyNuclear double resonance spectroscopyElectron paramagnetic resonance spectroscopyResonance spectroscopyParamagnetic resonance spectroscopyLow-temperature EPRO2 reduction siteDouble resonance spectroscopyReduction siteSpectroscopyCytochrome c oxidaseC oxidaseUnambiguous informationStructureEPRAmino acidsOxidaseOxideElucidationAcidNitric oxide
1982
The nature of CuA in cytochrome c oxidase.
Stevens T, Martin C, Wang H, Brudvig G, Scholes C, Chan S. The nature of CuA in cytochrome c oxidase. Journal Of Biological Chemistry 1982, 257: 12106-12113. PMID: 6288707, DOI: 10.1016/s0021-9258(18)33685-8.Peer-Reviewed Original ResearchConceptsCytochrome c oxidaseYeast cytochrome c oxidaseC oxidaseCysteine sulfurProteinBeef heartOxidaseElectron nuclear double resonance (ENDOR) spectraElectron paramagnetic resonanceSubstantial spin densityParamagnetic resonanceDouble resonance spectraBetaCuAResonance spectraCysteineSpin densityHistidine
1981
54 USE OF AN OPTIMIZED MITOCHONDRIAL PROTEIN SYNTHETIC SYSTEM TO CHARACTERIZE A PRECURSOR TO SUBUNIT II OF CYTOCHROME C OXIDASE
McKee E, Sevarino K, Bellus G, Poyton R. 54 USE OF AN OPTIMIZED MITOCHONDRIAL PROTEIN SYNTHETIC SYSTEM TO CHARACTERIZE A PRECURSOR TO SUBUNIT II OF CYTOCHROME C OXIDASE. 1981, 357-362. DOI: 10.1016/b978-0-08-025382-4.50059-9.Peer-Reviewed Original ResearchProtein synthetic systemCytochrome c oxidaseC oxidaseProtein synthesisMitochondrial translation productsCytoplasmic regulatory proteinsMaximal protein synthesisYeast mitochondriaCytoplasmic proteinsTranslation productsRegulatory proteinsSynthetic systemsMitochondriaProteinNucleotide concentrationsOxidaseSaccharomycesVivoPolypeptideOsmotic pressurePrevious studiesPrecursors
1980
Reactions of nitric oxide with cytochrome c oxidase.
Brudvig G, Stevens T, Chan S. Reactions of nitric oxide with cytochrome c oxidase. Biochemistry 1980, 19: 5275-85. PMID: 6255988, DOI: 10.1021/bi00564a020.Peer-Reviewed Original ResearchEvidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation
Brudvig G, Bocian D, Gamble R, Chan S. Evidence for the absence of photoreduction of the metal centers of cytochrome c oxidase by x-irradiation. Biochimica Et Biophysica Acta 1980, 624: 78-89. PMID: 6250634, DOI: 10.1016/0005-2795(80)90227-5.Peer-Reviewed Original ResearchConceptsConventional X-ray sourceStanford Synchrotron Radiation LaboratoryX-ray absorption measurementsX-ray photonsPhotons/sX-ray fluxX-ray sourcesSynchrotron Radiation LaboratoryMetal centerOptical spectroscopyRadiation LaboratoryAbsorption measurementsElectron paramagnetic resonanceParamagnetic resonanceCytochrome c oxidasePhotonsPhotoreductionC oxidaseRadiationResonanceSpectroscopyOxidaseSourceMeasurementsFluxPROTEIN PRECURSORS IN THE ASSEMBLY OF YEAST CYTOCHROME c OXIDASE, A TRANSMEMBRANOUS OLIGOMER OF THE INNER MITOCHONDRIAL MEMBRANE*
Poyton R, Sevarino K, George‐Nascimento C, Power S. PROTEIN PRECURSORS IN THE ASSEMBLY OF YEAST CYTOCHROME c OXIDASE, A TRANSMEMBRANOUS OLIGOMER OF THE INNER MITOCHONDRIAL MEMBRANE*. Annals Of The New York Academy Of Sciences 1980, 343: 275-292. PMID: 6249163, DOI: 10.1111/j.1749-6632.1980.tb47258.x.Peer-Reviewed Original ResearchMitochondrial membrane biogenesis: identification of a precursor to yeast cytochrome c oxidase subunit II, an integral polypeptide.
Sevarino K, Poyton R. Mitochondrial membrane biogenesis: identification of a precursor to yeast cytochrome c oxidase subunit II, an integral polypeptide. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 142-146. PMID: 6244538, PMCID: PMC348224, DOI: 10.1073/pnas.77.1.142.Peer-Reviewed Original ResearchConceptsMitochondrial translation productsInner mitochondrial membraneTranslation productsMitochondrial membraneIntegral polypeptidesCytochrome c oxidase subunit IIMitochondrial translation systemOligomeric enzyme complexesAurintricarboxylic acidNH2-terminal extensionCytochrome c oxidaseYeast mitochondriaInner membraneLeader sequenceSubunit IIEnzyme complexLarger precursorC oxidaseUnprocessed formPolypeptideTranslation systemMembraneTransient precursorNormal conditionsRibosomes
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