期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:2001
卷号:98
期号:24
页码:13649-13654
DOI:10.1073/pnas.241365698
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:F1-ATPase is a rotary motor enzyme in which a single ATP molecule drives a 120{degrees} rotation of the central {gamma} subunit relative to the surrounding 3{beta}3 ring. Here, we show that the rotation of F1-ATPase spontaneously lapses into long ({approx}30 s) pauses during steady-state catalysis. The effects of ADP-Mg and mutation on the pauses, as well as kinetic comparison with bulk-phase catalysis, strongly indicate that the paused enzyme corresponds to the inactive state of F1-ATPase previously known as the ADP-Mg inhibited form in which F1-ATPase fails to release ADP-Mg from catalytic sites. The pausing position of the {gamma} subunit deviates from the ATP-waiting position and is most likely the recently found intermediate 90{degrees} position.