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'Cytochrome Oxidase' in keywords
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1988 (1)
1982 (1)
1Author    MatildeBarón Ayala, Gerhard SandmannRequires cookie*
 Title    The Role of Cu in Respiration of Pea Plants and Heterotrophically Growing Scenedesmus Cells  
 Abstract    In Scenedesmus about half of NADH oxidation proceeds via a cyanide-sensitive and the other half via a cyanide-insensitive respiratory pathway. In contrast, respiration is completely cyanide sensitive in pea indicating that the alternative respiratory pathway is absent. Cu deficiency in pea plants and in heterotrophically grown Scenedesmus cells interferes with respiratory activity of mitochondria. In both organisms, the cyanide-sensitive NADH oxidation was strongly decreased during cultivation in low Cu media. Cu sensitivity was also observed for the alternative respiratory pathway in Scenedesmus. These results suggest that a Cu-containing component is involved in the alternative respiratory pathway. This is the main reason why alternative respiration cannot be regarded as a compensation for low cytochrome-oxidase activities during Cu starvation. The Cu dependency of the cyanide-sensitive respiration was located at the site of cytochrome oxidase. A strong coordination of the biosynthesis of the Cu-containing cytochrome-oxidase complex was evident. When the endogenous Cu pool was low, formation of cytochrome aa 3 , another component of cytochrome oxidase, was also decreased. 
  Reference    Z. Naturforsch. 43c, 438—442 (1988); received December 7 1987/February 10 1988 
  Published    1988 
  Keywords    Cu Deficiency, Cytochrome Oxidase, Mitochondria, Pea Plants, Scenedesmus 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0438.pdf 
 Identifier    ZNC-1988-43c-0438 
 Volume    43 
2Author    Hendrik Hüdig, Gerhart DrewsRequires cookie*
 Title    Isolation of a b-Type Cytochrome Oxidase from Membranes of the Phototrophic Bacterium Rhodopseudomonas capsulata  
 Abstract    A cytochrome oxidase (EC was solubilized from the membrane fraction o f aerobically grown cells of Rhodopseudomonas capsulata by treatment with Triton X-100. The enzyme was purified 160 fold by chromatography on DEAE-Sepharose CL -6B and affinity chromatography on cytochrome c-thiol activated Sepharose 4B. The purified enzyme has a pH-optimum at 8.5 and a temperature optimum at 35 °C. The ap­ parent K m for reduced horse cytochrome c is 24 |iM (at pH 8 and 30 °C). The purified cytochrome oxidase was 50% inhibited by 1.5 |iM KCN and 10 (iM N aN ,. The purified enzyme contained one polypeptide of mT 65,000 and 6-type cytochrome. 
  Reference    Z. Naturforsch. 37c, 193—198 (1982); received November 2 December 1 1981 
  Published    1982 
  Keywords    Rhodopseudomonas capsulata, Purification, Solubilization, Cytochrome c, Cytochrome Oxidase, 6-Type Cytochrome 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0193.pdf 
 Identifier    ZNC-1982-37c-0193 
 Volume    37