Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Comment
. 2023 Sep 29;4(6):zqad051.
doi: 10.1093/function/zqad051. eCollection 2023.

Elucidating a Complex Mechanism

Victor Wray  1
Affiliations
Comment

Elucidating a Complex Mechanism

Victor Wray. Function (Oxf). .
No abstract available

Keywords: ATP hydrolysis; Boyer’s binding change mechanism; F1-ATPase; Nath’s torsional mechanism; bi-site versus tri-site models of ATP synthesis/hydrolysis; ligand displacement.

PubMed Disclaimer

Conflict of interest statement

The author declares no competing interests.

Figures

Figure 1.
Figure 1.
New molecular mechanism of steady-state Vmax hydrolysis by F1-ATPase based on Nath’s torsional mechanism of energy transduction and ATP synthesis/hydrolysis. Boyer's binding change mechanism conceives that release of the product ADP results from binding of ATP to an allosteric site. On the basis of biochemical cold chase experiments, the new mechanism postulates activation by the simpler, more general explanation involving ligand displacement at a catalytic site of the F1-ATPase (panels 1 and 6 in Figure 1). For details, consult Nath (2023).
See this image and copyright information in PMC

Comment on

References

    1. Senior AE, Nadanaciva S, Weber J. The molecular mechanism of ATP synthesis by F1F0-ATP synthase. Biochim Biophys Acta Bioenerg. 2002;1553(3):188–211. - PubMed
    1. Nath S. The molecular mechanism of ATP synthesis by F1F0-ATP synthase: a scrutiny of the major possibilities. Adv Biochem Eng Biotechnol. 2002;74:65–98. doi: 10.1007/3-540-45736-4_4. - PubMed
    1. Nakano A, Kishikawa J, Nakanishi A, Mitsuoka K, Yokoyama K. Structural basis of unisite catalysis of bacterial F0F1-ATPase. PNAS Nexus. 2022;1(3):116–118. - PMC - PubMed
    1. Nakano A, Kishikawa J, Mitsuoka K, Yokoyama K. Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase. Nat Commun. 2023;14(1):4090. - PMC - PubMed
    1. Sobti M, Zeng YC, Walshe JL, Brown SHJ, Ishmukhametov R, Stewart AG. Changes within the central stalk of E. coli F1Fo ATP synthase observed after addition of ATP. Commun Biol. 2023;6(1):26. - PMC - PubMed

MeSH terms

Substances

LinkOut - more resources