Dirmeier, Reinhard and Keller, Martin and Frey, Gerhard and Huber, Harald and Stetter, Karl O. (1998) Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi. EUROPEAN JOURNAL OF BIOCHEMISTRY, 252 (3). pp. 486-491. ISSN 0014-2956
Full text not available from this repository.Abstract
The chemolithoautotrophic archaeon Pyrodictium abyssi isolate TAG 11 gains energy by reducing sulfur with H-2 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 H-2: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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | ARCHAEON PYROCOCCUS-FURIOSUS; SP-NOV REPRESENTS; WOLINELLA-SUCCINOGENES; ELECTRON-TRANSPORT; ELEMENTAL SULFUR; POLYSULFIDE REDUCTASE; ARCHAEBACTERIA; HYDROGENASE; RESPIRATION; GENUS; oxidoreductase; membrane bound; sulfur respiration; hyperthermophilic; Pyrodictium abyssi |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 28 Feb 2023 07:19 |
| Last Modified: | 28 Feb 2023 07:19 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50019 |
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