scholarly journals Preservation of NADH ubiquinone-oxidoreductase activity by Src kinase-mediated phosphorylation of NDUFB10

2012 ◽  
Vol 1817 (5) ◽  
pp. 718-725 ◽  
Author(s):  
Etienne Hebert-Chatelain ◽  
Caroline Jose ◽  
Nicolas Gutierrez Cortes ◽  
Jean-William Dupuy ◽  
Christophe Rocher ◽  
...  
Keyword(s):  
Src Kinase ◽  
Oxidoreductase Activity ◽  
Ubiquinone Oxidoreductase ◽  
Nadh Ubiquinone Oxidoreductase

scholarly journals NN′-dicyclohexylcarbodi-imide-sensitivity of bovine heart mitochondrial NADH: ubiquinone oxidoreductase. Inhibition of activity and binding to subunits

1988 ◽  
Vol 249 (2) ◽  
pp. 339-344 ◽  
Author(s):  
P T Vuokila ◽  
I E Hassinen
Keyword(s):  
Time Course ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Dependent Manner ◽  
Submitochondrial Particles ◽  
Concentration Dependent Manner ◽  
Oxidoreductase Activity ◽  
Ubiquinone Oxidoreductase ◽  
Nadh Ubiquinone Oxidoreductase ◽  
Electron And Proton Transport ◽  
Molecular Masses

Dicyclohexylcarbodi-imide (DCCD) inhibition of NADH: ubiquinone oxidoreductase was studied in submitochondrial particles and in the isolated form, together with the binding of the reagent to the enzyme. DCCD inhibited the isolated enzyme in a time- and concentration-dependent manner. Over the concentration range studied, a maximum inhibition of 85% was attained within 60 min. The time course for the binding of DCCD to the enzyme was similar to that of activity inhibition. The NADH:ubiquinone oxidoreductase activity of the submitochondrial particles was also sensitive to DCCD, and the locus of binding of the inhibitor was studied by subsequent resolution of the enzyme into subunit polypeptides. Only two subunits (molecular masses 13.7 and 21.5 kDa) were labelled by [14C]DCCD, whereas, when the enzyme in its isolated form was treated with [14C]DCCD, six subunits (13.7, 16.1, 21.5, 39, 43 and 53 kDa) were labelled. Comparison with the subunit labelling of F1F0-ATPase and ubiquinol:cytochrome c oxidoreductase indicated that the labelling pattern of NADH:ubiquinone oxidoreductase, and enzyme complex with a multitude of subunits, is unique and not due to contamination by other inner-membrane proteins. The correlation between the electron- and proton-transport functions and the DCCD-binding components remains to be established.

scholarly journals The interaction between mitochondrial NADH-ubiquinone oxidoreductase and ubiquinol-cytochrome c oxidoreductase. Evidence for stoicheiometric association

1978 ◽  
Vol 174 (3) ◽  
pp. 783-790 ◽  
Author(s):  
C I Ragan ◽  
C Heron
Keyword(s):  
Cytochrome C ◽  
Complex I ◽  
Structural Features ◽  
Complex Iii ◽  
Molar Ratio ◽  
Oxidoreductase Activity ◽  
Ubiquinone Oxidoreductase ◽  
Nadh Ubiquinone Oxidoreductase ◽  
Cytochrome C Reduction ◽  
Nadh Cytochrome

1. The NADH-ubiquinone oxidoreductase complex (Complex I) and the ubiquinol-cytochrome c oxidoreductase complex (Complex III) combine in a 1:1 molar ratio to give NADH-cytochrome c oxidoreductase (Complex I-Complex III). 2. Experiments on the inhibition of the NADH-cytochrome c oxidoreductase activity of mixtures of Complexes I and III by rotenone and antimycin indicate that electron transfer between a unit of Complex I-Complex III and extra molecules of Complexes I or III does not contribute to the overall rate of cytochrome c reduction. 3. The reduction by NADH of the cytochrome b of mixtures of Complexes I and III is biphasic. The extents of the fast and slow phases of reduction are determined by the proportion of the total Complex III specifically associated with Complex I. 4. Activation-energy measurements suggest that the structural features of the Complex I-Complex III unit promote oxidoreduction of endogenous ubiquinone-10.

scholarly journals Photoaffinity labelling of mitochondrial NADH dehydrogenase with arylazidoamorphigenin, an analogue of rotenone

1984 ◽  
Vol 224 (2) ◽  
pp. 525-534 ◽  
Author(s):  
F G P Earley ◽  
C I Ragan
Keyword(s):  
Nadh Dehydrogenase ◽  
Oxidoreductase Activity ◽  
Photoaffinity Labelling ◽  
Ubiquinone Oxidoreductase ◽  
Naturally Occurring ◽  
Respiratory Inhibitor ◽  
Nadh Ubiquinone Oxidoreductase ◽  
Low Concentrations ◽  
Preferential Incorporation ◽  
Parallel Fashion

A photoaffinity-labelling analogue of the respiratory inhibitor rotenone was synthesized from the naturally occurring rotenoid amorphigenin. The analogue inhibits NADH-ubiquinone oxidoreductase activity at concentrations comparable with those of rotenone. Photolysis of the radiolabelled analogue bound to isolated NADH-ubiquinone oxidoreductase resulted in preferential incorporation of radioactivity into a polypeptide of Mr 33 000, particularly at low concentrations of the inhibitor. Preparations of the enzyme differ in a parallel fashion in the content of this polypeptide, the degree of photolabelling by the analogue and their sensitivity to rotenone, providing further evidence that the 33 000-Mr protein forms part of the rotenone-binding site.

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