Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi

被引:30
作者
Dirmeier, R [1 ]
Keller, M [1 ]
Frey, G [1 ]
Huber, H [1 ]
Stetter, KO [1 ]
机构
[1] Lehrstuhl Mikrobiol, D-93053 Regensburg, Germany
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1998年 / 252卷 / 03期
关键词
oxidoreductase; membrane bound; sulfur respiration; hyperthermophilic; Pyrodictium abyssi;
D O I
10.1046/j.1432-1327.1998.2520486.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:486 / 491
页数:6
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