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1981 (1)
1Author    Toshihisa Ohshima, Gerhart DrewsRequires cookie*
 Title    Isolation and Partial Characterization of the Membrane-Bound NADH Dehydrogenase from the Phototrophic Bacterium Rhodopseudomonas capsulata  
 Abstract    Chem otrophically grown cells of Rhodopseudomonas capsulata contain at least three different pyridine nucleotide dehydrogenases, i) a soluble, found in the supernatant (144000 x g) o f cell free extracts, N AD H-dependent, ii) a mem brane-bound, N AD H -dependent, and iii) a soluble, found in the supernatant N AD PH dependent. i The m em brane-bound N A D H dehydrogenase (E.C. 1.6.99.3) has been solubilized by sodium deoxycholate treatm ent of m em branes and purified 75 fold by column chrom atography on Sephadex G-150 and DEAE cellulose in the presence of sodium cholate. The native enzyme has an apparent molecular mass (M r) o f 97 000, containing polypeptides of Mr of about 15 000. The pH optim um was at 7.5. The enzyme was specific for NADH. The Michaelis constant for NADH and DCIP were 4.0 and 63 hm, respectively. The enzyme was inactivated by FM N, riboflavin and NADH. In contrast, the soluble N ADH-dehydrogenase (i) was activated by FMN. 
  Reference    Z. Naturforsch. 36c, 400 (1981); received February 23/M arch 16 1981 
  Published    1981 
  Keywords    NADH Dehydrogenase, Purification, Localization, Inhibitors, Rhodopseudomonas capsulata 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0400.pdf 
 Identifier    ZNC-1981-36c-0400 
 Volume    36