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The βG 156 C Substitution in the F 1 -ATPase from the Thermophilic Bacillus PS3 Affects Catalytic Site Cooperativity by Destabilizing the Closed Conformation of the Catalytic Site †

✍ Scribed by Bandyopadhyay, Sanjay; Valder, Carolina R.; Huynh, Hue G.; Ren, Huimiao; Allison, William S.


Book ID
127334548
Publisher
American Chemical Society
Year
2002
Tongue
English
Weight
170 KB
Volume
41
Category
Article
ISSN
0006-2960

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✍ Jault, Jean-Michel; Matsui, Tadashi; Jault, Francoise M.; Kaibara, Chitose; Mune 📂 Article 📅 1995 🏛 American Chemical Society 🌐 English ⚖ 891 KB

ATP hydrolyses by the wild-type a&y and mutant (aD261N)3P3y subcomplexes of the FI-ATPase from the thermophilic Bacillus PS3 have been compared. The wild-type complex hydrolyzes 50 p M ATP in three kinetic phases: a burst decelerates to an intermediate phase, which then gradually accelerates to a fi