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Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi.
Dirmeier, R; Keller, M; Frey, G; Huber, H; Stetter, K O.
Afiliación
  • Dirmeier R; Lehrstuhl für Mikrobiologie, Regensburg, Germany. reinhard.dirmeier@biologie.uni-regensburg.de
Eur J Biochem ; 252(3): 486-91, 1998 Mar 15.
Article en En | MEDLINE | ID: mdl-9546664
The chemolithoautotrophic archaeon Pyrodictium abyssi isolate TAG 11 gains energy by reducing sulfur with H2 to H2S. From this hyperthermophile, a sulfur-reducing complex catalyzing this reaction was purified 13.5-fold. The native complex exhibited a brownish-yellow colour and showed an apparent molecular mass of 520 kDa. SDS/PAGE revealed the presence of nine different major polypeptides with apparent molecular masses of 82, 72, 65, 50, 47, 42, 40, 30 and 24 kDa. The native complex contained 50-55 mol acid-labile sulfur, 50-55 mol iron, 1.6 mol nickel, 1.2 mol copper, 2.8 mol cytochrome b and 0.3 mol cytochrome c (all per mol native complex). The temperature optimum of the H2:sulfur oxidoreductase complex was 100 degrees C, which is consistent with the physiological growth optimum of the native organism. The complex is extremely heat stable. During 5 h incubation at 100 degrees C, no decrease in H2S-forming activity could be observed.
Asunto(s)
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oxidorreductasas / Azufre / Desulfurococcaceae / Complejos Multienzimáticos Idioma: En Revista: Eur J Biochem Año: 1998 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oxidorreductasas / Azufre / Desulfurococcaceae / Complejos Multienzimáticos Idioma: En Revista: Eur J Biochem Año: 1998 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido