The N-terminal region of the ε subunit from cyanobacterial ATP synthase alone can inhibit ATPase activity
Author:
Funder
MEXT | Japan Society for the Promotion of Science (JSPS)
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference54 articles.
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3. The FOF1 ATP synthase: from atomistic three-dimensional structure to the rotary-chemical function;Mukherjee;Photosynth. Res,2017
4. Subunit structure of adenosine triphosphatase: comparison of the structure in thermophilic bacterium PS3 with those in mitochondria, chloroplasts, and Escherichia coli;Yoshida;J. Biol. Chem,1979
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1. Structure, Regulation, and Significance of Cyanobacterial and Chloroplast Adenosine Triphosphate Synthase in the Adaptability of Oxygenic Photosynthetic Organisms;Microorganisms;2024-05-06
2. The phototroph-specific β-hairpin structure of the γ subunit of FoF1-ATP synthase is important for efficient ATP synthesis of cyanobacteria;Journal of Biological Chemistry;2021-09
3. F-ATP-ase of Escherichia coli membranes: The ubiquitous MgADP-inhibited state and the inhibited state induced by the ε–subunit's C-terminal domain are mutually exclusive;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2020-07
4. Regulation machineries of ATP synthase from phototroph;Advances in Botanical Research;2020
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