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dc.contributor.authorBabot, M.
dc.contributor.authorLabarbuta, P.
dc.contributor.authorBirch, Amanda
dc.contributor.authorKee, S.
dc.contributor.authorFuszard, M.
dc.contributor.authorBotting, C.H.
dc.contributor.authorWittig, I.
dc.contributor.authorHeide, H.
dc.contributor.authorGalkin, A.
dc.identifier.citationBabot , M , Labarbuta , P , Birch , A , Kee , S , Fuszard , M , Botting , C H , Wittig , I , Heide , H & Galkin , A 2014 , ' ND3, ND1 and 39 kDa subunits are more exposed in the de-active form of bovine mitochondrial complex i ' , Biochimica et Biophysica Acta - Bioenergetics , vol. 1837 , no. 6 , pp. 929-939 .
dc.identifier.otherPURE: 118139142
dc.identifier.otherPURE UUID: 6461fbc7-7410-47fe-bec6-6599aa7a143b
dc.identifier.otherScopus: 84897352802
dc.identifier.otherWOS: 000337013500022
dc.descriptionThis study was supported by MRC grants G1100051 (to A.G.) and by the Cluster of Excellence “Macromolecular Complexes” at the Goethe University Frankfurt [EXC 115], the Deutsche Forschungsgemeinschaft Sonderforschungsbereich 815 project Z1-Redox-Proteomics and by the Bundesministerium für Bildung und Forschung Grant BMBF [01GM1113B] mitoNET-Deutsches Netzwerk für mitochondriale Erkrankungen (to I.W.).en
dc.description.abstractAn intriguing feature of mitochondrial complex I from several species is the so-called A/D transition, whereby the idle enzyme spontaneously converts from the active (A) form to the de-active (D) form. The A/D transition plays an important role in tissue response to the lack of oxygen and hypoxic deactivation of the enzyme is one of the key regulatory events that occur in mitochondria during ischaemia. We demonstrate for the first time that the A/D conformational change of complex I does not affect the macromolecular organisation of supercomplexes in vitro as revealed by two types of native electrophoresis. Cysteine 39 of the mitochondrially-encoded ND3 subunit is known to become exposed upon de-activation. Here we show that even if complex I is a constituent of the I + III + IV (S) supercomplex, cysteine 39 is accessible for chemical modification in only the D-form. Using lysine-specific fluorescent labelling and a DIGE-like approach we further identified two new subunits involved in structural rearrangements during the A/D transition: ND1 (MT-ND1) and 39 kDa (NDUFA9). These results clearly show that structural rearrangements during de-activation of complex I include several subunits located at the junction between hydrophilic and hydrophobic domains, in the region of the quinone binding site. De-activation of mitochondrial complex I results in concerted structural rearrangement of membrane subunits which leads to the disruption of the sealed quinone chamber required for catalytic turnover. Crown
dc.relation.ispartofBiochimica et Biophysica Acta - Bioenergeticsen
dc.rightsCrown Copyright © 2014 Published by Elsevier B.V. All rights reserved.en
dc.subjectComplex Ien
dc.subjectNADH:ubiquinone oxidoreductaseen
dc.subjectA/D transitionen
dc.subjectConformational changeen
dc.subjectProtein tyrosine modificationen
dc.subjectN -hydroxysuccinimideen
dc.subjectQH301 Biologyen
dc.titleND3, ND1 and 39 kDa subunits are more exposed in the de-active form of bovine mitochondrial complex ien
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Chemistryen
dc.contributor.institutionUniversity of St Andrews. EaSTCHEMen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.description.statusPeer revieweden

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