Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated beta subunit of the F0.F1 ATP synthase is a catalytic site.-Reference-Cited by-同舟云学术

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Evidence that the Mg-dependent low-affinity binding site for ATP and Pi demonstrated on the isolated beta subunit of the F0.F1 ATP synthase is a catalytic site.

Published:1985-04-01 Issue:7 Volume:82 Page:1886-1890
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Khananshvili D.,Gromet-Elhanan Z.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Cited by 45 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

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2. The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology;Physiological Reviews;2015-10

3. Catalysis by isolated β-subunits of the ATP Synthase/ATPase from Thermophilic bacillus PS3. Hydrolysis of Pyrophosphate;Journal of Bioenergetics and Biomembranes;2008-12

4. ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas;Microbiology and Molecular Biology Reviews;2008-12

5. Association of α-Subunits with Nucleotide-Modified β-Subunits Induces Asymmetry in the Catalytic Sites of the F₁-ATPase α₃β₃-Hexamer;Cell Biochemistry and Biophysics;2003

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