Your browser doesn't support javascript.
loading
Association of 2-oxoacid dehydrogenase complexes with respirasomes in mitochondria.
Plokhikh, Konstantin S; Nesterov, Semen V; Chesnokov, Yuriy M; Rogov, Anton G; Kamyshinsky, Roman A; Vasiliev, Aleksandr L; Yaguzhinsky, Lev S; Vasilov, Raif G.
Afiliación
  • Plokhikh KS; Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, Moscow, Russia.
  • Nesterov SV; Shubnikov Institute of Crystallography, Federal Scientific Research Centre "Crystallography and Photonics" of Russian Academy of Sciences, Moscow, Russia.
  • Chesnokov YM; Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, Moscow, Russia.
  • Rogov AG; Moscow Institute of Physics and Technology, Dolgoprudny, Russia.
  • Kamyshinsky RA; Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, Moscow, Russia.
  • Vasiliev AL; Shubnikov Institute of Crystallography, Federal Scientific Research Centre "Crystallography and Photonics" of Russian Academy of Sciences, Moscow, Russia.
  • Yaguzhinsky LS; Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, Moscow, Russia.
  • Vasilov RG; Kurchatov Complex of NBICS-Technologies, National Research Center Kurchatov Institute, Moscow, Russia.
FEBS J ; 291(1): 132-141, 2024 01.
Article en En | MEDLINE | ID: mdl-37789611
In the present study, cryo-electron tomography was used to investigate the localization of 2-oxoacid dehydrogenase complexes (OADCs) in cardiac mitochondria and mitochondrial inner membrane samples. Two classes of ordered OADC inner cores with different symmetries were distinguished and their quaternary structures modeled. One class corresponds to pyruvate dehydrogenase complexes and the other to dehydrogenase complexes of α-ketoglutarate and branched-chain α-ketoacids. OADCs were shown to be localized in close proximity to membrane-embedded respirasomes, as observed both in densely packed lamellar cristae of cardiac mitochondria and in ruptured mitochondrial samples where the dense packing is absent. This suggests the specificity of the OADC-respirasome interaction, which allows localized NADH/NAD+ exchange between OADCs and complex I of the respiratory chain. The importance of this local coupling is based on OADCs being the link between respiration, glycolysis and amino acid metabolism. The coupling of these basic metabolic processes can vary in different tissues and conditions and may be involved in the development of various pathologies. The present study shows that this important and previously missing parameter of mitochondrial complex coupling can be successfully assessed using cryo-electron tomography.
Asunto(s)
Palabras clave

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Complejo Piruvato Deshidrogenasa / Cetoácidos Tipo de estudio: Risk_factors_studies Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Complejo Piruvato Deshidrogenasa / Cetoácidos Tipo de estudio: Risk_factors_studies Idioma: En Revista: FEBS J Asunto de la revista: BIOQUIMICA Año: 2024 Tipo del documento: Article País de afiliación: Rusia Pais de publicación: Reino Unido