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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

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