Electron Transport and Oxidative Phosphorylation
Electron Transport and Oxidative Phosphorylation
Electron Transport and Oxidative Phosphorylation
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Figure 20.27<br />
The binding change mechanism for<br />
ATP synthesis by ATP synthase.<br />
This model assumes that F 1 has<br />
three interacting <strong>and</strong><br />
conformationally distinct active sites.<br />
The open (O) conformation is<br />
inactive <strong>and</strong> has a low affinity for<br />
lig<strong>and</strong>s; the L conformation (with<br />
“loose” affinity for lig<strong>and</strong>s) is also<br />
inactive; the tight (T) conformation is<br />
active <strong>and</strong> has a high affinity for<br />
lig<strong>and</strong>s. Synthesis of ATP is initiated<br />
(step 1) by binding of ADP <strong>and</strong> Pi to<br />
an L site. In the second step, an<br />
energy-driven conformational<br />
change converts the L site to a T<br />
conformation <strong>and</strong> also converts T to<br />
O <strong>and</strong> O to L. In the third step, ATP<br />
is synthesized at the T site <strong>and</strong><br />
released from the O site. Two<br />
additional passes through this cycle<br />
produce two more ATPs <strong>and</strong> return<br />
the enzyme to its original state.<br />
Garrett <strong>and</strong> Grisham, Biochemistry, Third Edition