Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Seiga, Yanagisawa"'
Publikováno v:
Frontiers in Molecular Biosciences, Vol 11 (2024)
Vacuolar ATP-dependent proton pumps (V-ATPases) belong to a super-family of rotary ATPases and ATP synthases. The V1 complex consumes ATP to drive rotation of a central rotor that pumps protons across membranes via the Vo complex. Eukaryotic V-ATPase
Externí odkaz:
https://doaj.org/article/7f33785dbbe843e9b60ea697e096266a
Publikováno v:
Frontiers in Microbiology, Vol 13 (2022)
The F-ATP synthase, consisting of F1 and FO motors connected by a central rotor and the stators, is the enzyme responsible for synthesizing the majority of ATP in all organisms. The F1 (αβ)3 ring stator contains three catalytic sites. Single-molecu
Externí odkaz:
https://doaj.org/article/0a0eae7706e64ebcaba4cfca72cf604d
Autor:
Seiga Yanagisawa, Wayne D Frasch
Publikováno v:
eLife, Vol 10 (2021)
Most cellular ATP is made by rotary F1FO ATP synthases using proton translocation-generated clockwise torque on the FO c-ring rotor, while F1-ATP hydrolysis can force counterclockwise rotation and proton pumping. The FO torque-generating mechanism re
Externí odkaz:
https://doaj.org/article/895a97d7a02245d6ae81456adbeb6406
Publikováno v:
Molecules, Vol 24, Iss 3, p 504 (2019)
F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F1 domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)3δab2. Subunits c10 or (αβ)3 alone are rotationally symmetric. H
Externí odkaz:
https://doaj.org/article/ef8643f45cef41e886da790a759eb0f0
Publikováno v:
Frontiers in microbiology. 13
The F-ATP synthase, consisting of F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f246b981db0c9340cfaa7134c7bab95f
https://pubmed.ncbi.nlm.nih.gov/36081786
https://pubmed.ncbi.nlm.nih.gov/36081786
pH-dependent 11° F1 FO ATP synthase sub-steps reveal insight into the FO torque generating mechanism.
Autor:
Seiga Yanagisawa, Frasch, Wayne D.
Publikováno v:
eLife; 1/12/2022, p1-20, 20p
Publikováno v:
Molecules, Vol 24, Iss 3, p 504 (2019)
Molecules
Molecules
F-ATP synthases use proton flow through the FO domain to synthesize ATP in the F1 domain. In Escherichia coli, the enzyme consists of rotor subunits γεc10 and stator subunits (αβ)3δab2. Subunits c10 or (αβ)3 alone are rotationally symmetric. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ab4e07fc852d18c9c2235053e1cfb6
https://www.mdpi.com/1420-3049/24/3/504
https://www.mdpi.com/1420-3049/24/3/504
Autor:
Wayne D. Frasch, Seiga Yanagisawa
The two opposed rotary molecular motors of the F0F1-ATP synthase work together to provide the majority of ATP in biological organisms. Rotation occurs in 120° power strokes separated by dwells when F1 synthesizes or hydrolyzes ATP. F0 and F1 complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::902228d1b399204065fa3118bfd1e5dc
https://europepmc.org/articles/PMC5641864/
https://europepmc.org/articles/PMC5641864/
Autor:
Seiga Yanagisawa1, Frasch, Wayne D.1 frasch@asu.edu
Publikováno v:
Journal of Biological Chemistry. 10/13/2017, Vol. 292 Issue 41, p17093-17100. 8p.