Editing ATP synthase (section)

=== F<sub>1</sub> region ===
The F<sub>1</sub> portion of ATP synthase is [[hydrophilic]] and responsible for hydrolyzing ATP. The F<sub>1</sub> unit protrudes into the [[mitochondrial matrix]] space. Subunits α and β make a hexamer with 6 binding sites. Three of them are catalytically inactive and they bind ADP.

Three other subunits catalyze the ATP synthesis. The other F<sub>1</sub> subunits γ, δ, and ε are a part of a rotational motor mechanism (rotor/axle). The γ subunit allows β to go through conformational changes (i.e., closed, half open, and open states) that allow for ATP to be bound and released once synthesized. The F<sub>1</sub> particle is large and can be seen in the transmission electron microscope by negative staining.<ref>{{cite journal | vauthors = Fernandez Moran H, Oda T, Blair PV, Green DE | title = A macromolecular repeating unit of mitochondrial structure and function. Correlated electron microscopic and biochemical studies of isolated mitochondria and submitochondrial particles of beef heart muscle | journal = The Journal of Cell Biology | volume = 22 | issue = 1 | pages = 63–100 | date = July 1964 | pmid = 14195622 | pmc = 2106494 | doi = 10.1083/jcb.22.1.63 }}</ref> These are particles of 9&nbsp;nm diameter that pepper the inner mitochondrial membrane.

{| class="wikitable" style="text-align:center"
|+ F<sub>1</sub> – Subunits<ref name=pmid24878343/>

|-
! Subunit !! Human Gene !! Note
|-
| [[ATP synthase alpha/beta subunits|alpha]] || ''[[ATP5A1]]'', ''[[ATPAF2]]'' ||
|-
| [[ATP synthase alpha/beta subunits|beta]] || ''[[ATP5B]]'', ''[[ATPAF1]]'' ||
|-
| [[ATP synthase gamma subunit|gamma]] || ''[[ATP5C1]]'' ||
|-
| [[ATP synthase delta/epsilon subunit|delta]] || ''[[ATP5D]]'' || Mitochondrial "delta" is bacterial/chloroplastic epsilon.
|-
| [[ATP synthase epsilon subunit, mitochondrial|epsilon]] || ''[[ATP5E]]'' || Unique to mitochondria.
|-
| [[ATP synthase delta/OSCP subunit|OSCP]] || ''[[ATP5O]]'' || Called "delta" in bacterial and chloroplastic versions.
|}