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：1999
卷号：96
期号：14
页码：7780-7784
DOI：10.1073/pnas.96.14.7780
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：The rotation of the {gamma}-subunit has been included in the binding-change mechanism of ATP synthesis/hydrolysis by the proton ATP synthase (FOF1). The Escherichia coli ATP synthase was engineered for rotation studies such that its ATP hydrolysis and synthesis activity is similar to that of wild type. A fluorescently labeled actin filament connected to the {gamma}-subunit of the F1 sector rotated on addition of ATP. This progress enabled us to analyze the {gamma}M23K (the {gamma}-subunit Met-23 replaced by Lys) mutant, which is defective in energy coupling between catalysis and proton translocation. We found that the F1 sector produced essentially the same frictional torque, regardless of the mutation. These results suggest that the {gamma}M23K mutant is defective in the transformation of the mechanical work into proton translocation or vice versa.
