Oxidative Phosphorylation, Part I

Flashcards covering the structure and function of ATP synthase, the binding-change mechanism, and the components of oxidative phosphorylation as detailed in the lecture.

F1 component

The catalytic part of ATP synthase that contains three catalytic $\beta$ subunits and resides in the mitochondrial matrix.

F0 component

The portion of ATP synthase that is embedded in the inner mitochondrial membrane and contains the proton channel.

c ring

A rotational component of the $F_0$ unit driven by the motion of protons across the membrane.

O (open) form

A conformation of the $\beta$ subunit where nucleotides can bind to or be released from the subunit.

L (loose) form

A conformation of the $\beta$ subunit where nucleotides are trapped within the subunit.

T (tight) form

A conformation of the $\beta$ subunit where ATP is synthesized from ADP and $P_i$.

Binding-change mechanism

The mechanism that accounts for the synthesis of ATP in response to proton flow through the rotational movement of the $\gamma$ subunit.

Stator

Also known as the peripheral stalk, this structure stabilizes the $\alpha_3\beta_3$ hexamer and prevents it from rotating.

Rotor

The moving part of ATP synthase consisting of the c-ring and the central stalk (composed of $\gamma$ and $\epsilon$ subunits).

Vertebrate c ring

A structure consisting of $8$ subunits, making vertebrate ATP synthase the most efficient known.

Proton-motive force

The electrochemical gradient established by the electron-transport chain that drives the rotation of the c ring to synthesize ATP.

Cristae

Folds of the inner mitochondrial membrane whose formation is assisted by ATP synthase.

Central stalk

Part of the rotor, specifically the $\gamma$ and $\epsilon$ subunits, that rotates to induce conformational changes in the $\beta$ subunits.