Enzyme-bound ATP is released

Stable Identifier
R-HSA-164834
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
In the last step, the beta subunit is converted to the open form and ATP is released. Passage of protons through the Fo part causes a ring of approximately 10 subunits to rotate. This rotation in turn drives the rotation of the gamma subunits, which forms part of one of the stalks. The gamma subunit moves between the three beta subunits which are held in place by the second stalk which can be regarded as a stator. The polypeptide called OSCP connects the stator stalk to the assembly of alpha and beta subunits. It is this step that is coupled to proton translocation as energy is required to break the strong bond between ATP and the protein.
Literature References
PubMed ID Title Journal Year
4517936 A new concept for energy coupling in oxidative phosphorylation based on a

Boyer, PD, Momsen, W, Cross, RL

Proc Natl Acad Sci U S A 1973
Participants
Participates
Event Information
Catalyst Activity

proton transmembrane transporter activity of ATPase:ATP [mitochondrial inner membrane]

Orthologous Events
Authored
Created
Cite Us!