Characterization of the 25-kilodalton subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans: sequence similarity to the 24-kilodalton subunit of the flavoprotein fraction of mammalian complex I

Biochemistry ◽  
1991 ◽  
Vol 30 (35) ◽  
pp. 8678-8684 ◽  
Author(s):  
Xuemin Xu ◽  
Akemi Matsuno-Yagi ◽  
Takao Yagi
Biochemistry ◽  
2008 ◽  
Vol 47 (40) ◽  
pp. 10816-10826 ◽  
Author(s):  
Naoya Ichimaru ◽  
Masatoshi Murai ◽  
Nobuyuki Kakutani ◽  
Junko Kako ◽  
Atsushi Ishihara ◽  
...  

1987 ◽  
Vol 244 (3) ◽  
pp. 661-668 ◽  
Author(s):  
C L George ◽  
S J Ferguson

Monospecific antibody to the respiratory NADH dehydrogenase from Paracoccus denitrificans was prepared by using as antigen specific immunoprecipitates containing NADH dehydrogenase which were excised from crossed-immunoelectrophoresis plates. The latter were run with selectively solubilized plasma membranes and antibodies against plasma membranes. The antibody immunoprecipitated NADH dehydrogenase from P. denitrificans membranes biosynthetically labelled with 14C and solubilized with a wide range of detergents. All immunoprecipitates contained the two subunits of Mr 48,000 and 25,000, in an approximate 1:1 stoichiometry, that had previously been assigned to NADH dehydrogenase. A polypeptide of Mr 46,000 in P. denitrificans membranes, previously shown to cross-react with a subunit-specific antibody to mitochondrial NADH dehydrogenase (complex I), was not detected in any immunoprecipitate. Under some conditions a third polypeptide, of Mr 31,000, was also detected, but in variable and non-stoichiometric amounts relative to the two other subunits. It was concluded that this polypeptide was incorporated into the immunoprecipitates as an artefact and that the polypeptides of Mr 48,000 and 25,000 are the sole polypeptides firmly identified in the NADH dehydrogenase. Flavoproteins were specifically radiolabelled by growth of P. denitrificans in the presence of [14C]riboflavin. Crossed immunoelectrophoresis of membranes from such cells showed that succinate dehydrogenase contained flavin, but that there was no detectable flavin in NADH dehydrogenase under these conditions. Analysis of excised immunoprecipitates of succinate dehydrogenase showed that flavin was covalently bound to a polypeptide of Mr 56,000. Flavin was retained by NADH dehydrogenase under mild conditions of detergent solubilization. Subsequent immunoprecipitation, followed by analysis of the acid-extracted flavin, established that FMN is a cofactor, in common with mitochondrial NADH-ubiquinone oxidoreductase (complex I).


2000 ◽  
Vol 75 (1) ◽  
pp. 383-392 ◽  
Author(s):  
Edward H. Pettus ◽  
Ranjita Betarbet ◽  
Barbara Cottrell ◽  
Douglas C. Wallace ◽  
Vijay Madyastha ◽  
...  

1994 ◽  
Vol 22 (1) ◽  
pp. 226-230 ◽  
Author(s):  
Thorsten Friedrich ◽  
Tomoko Ohnishi ◽  
Edgar Forche ◽  
Brigitte Kunze ◽  
Rolf Jansen ◽  
...  

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