Das A, Ljungdahl L G
Center for Biological Resource Recovery, University of Georgia, Athens 30602.
FEBS Lett. 1993 Feb 8;317(1-2):17-21. doi: 10.1016/0014-5793(93)81482-f.
F1-stripped membrane vesicles from Clostridium thermoautotrophicum and Escherichia coli were reconstituted with F1-ATPases from both bacteria. Reconstituted F1F0-ATPase complexes were catalytically active, i.e. capable of hydrolyzing ATP. Homologous-type ATPase complexes having F0 and F1 parts of ATP synthases from the same origin were DCCD sensitive and supported ATP-driven enhancement of anilinonaphthalene sulfonate (ANS) fluorescence. Hybrid-type ATPase complexes having F0 and F1 parts of ATP synthases from different origins were neither DCCD sensitive nor did they support ATP-driven enhancement of ANS fluorescence. Analyzing these results it has been demonstrated that the F0 and F1 parts of ATP synthases of these two bacteria are not functionally compatible.
将来自嗜热自养梭菌和大肠杆菌的F1剥离膜囊泡与这两种细菌的F1 - ATP酶进行重组。重组后的F1F0 - ATP酶复合物具有催化活性，即能够水解ATP。具有来自同一来源的ATP合酶的F0和F1部分的同源型ATP酶复合物对二环己基碳二亚胺（DCCD）敏感，并支持ATP驱动的苯胺萘磺酸盐（ANS）荧光增强。具有来自不同来源的ATP合酶的F0和F1部分的杂交型ATP酶复合物既对DCCD不敏感，也不支持ATP驱动的ANS荧光增强。通过分析这些结果表明，这两种细菌的ATP合酶的F0和F1部分在功能上不兼容。
