嗜热自养甲烷杆菌膜结合ATP合酶复合物进行的ATP水解与合成
ATP hydrolysis and synthesis by the membrane-bound ATP synthetase complex of Methanobacterium thermoautotrophicum.
作者信息
Doddema H J, Hutten T J, van der Drift C, Vogels G D
出版信息
J Bacteriol. 1978 Oct;136(1):19-23. doi: 10.1128/jb.136.1.19-23.1978.
Abstract
The membrane-bound ATP synthetase complex of Methanobacterium thermoautotrophicum showed maximum activity for ATP hydrolysis at pH 8, at temperatures between 65 and 70 degrees C, and at an ATP-Mg2+ ratio of 0.5. Anaerobic conditions were not prerequisite for enzyme activity. The enzyme showed a Km value for ATP of 2 mM, and activity was Mg2+ dependent; Mn2+, Co2+, Ca2+, and Zn2+ could replace Mg2+ to some extent. Other nucleoside triphosphates could be hydrolyzed. N,N'-dicyclohexylcarbodiimide inhibited ATP hydrolysis. A proton-motive force, artificially imposed by a pH shift or valinomycin, resulted in ATP synthesis in whole cells. The ATP synthetase complex of the thermophilic methanogenic bacterium is similar to those described in aerobic and anaerobic microorganisms.
摘要
嗜热自养甲烷杆菌的膜结合ATP合酶复合体在pH 8、65至70摄氏度的温度以及ATP与Mg2+比例为0.5时，ATP水解活性最高。厌氧条件并非酶活性的先决条件。该酶对ATP的Km值为2 mM，活性依赖于Mg2+；Mn2+、Co2+、Ca2+和Zn2+在一定程度上可以替代Mg2+。其他核苷三磷酸也可被水解。N，N'-二环己基碳二亚胺抑制ATP水解。由pH变化或缬氨霉素人为施加的质子动力导致全细胞中ATP的合成。嗜热产甲烷细菌的ATP合酶复合体与需氧和厌氧微生物中描述的类似。
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