4.06:_ATP_Synthase

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<p class="lt-bio-4632" style="background-color: unset;">ATP synthase is a huge molecular complex (&gt;500,000 daltons) embedded in the inner membrane of mitochondria. Its function is to convert the energy of protons (H<sup><font size="2">+</font></sup>) moving down their concentration gradient into the synthesis of ATP. 3 to 4 protons moving through this machine is enough to convert a molecule of ADP and P<sub><font size="2">i</font></sub> (inorganic phosphate) into a molecule of ATP. One ATP synthase complex can generate &gt;100 molecules of ATP each second.</p>

<figure><img class="internal" alt="Diagram of ATP synthase in the inner mitochondrial membrane, showing proton flow from intermembrane space to matrix, driving ATP production. Uncouplers and inhibitors are labeled." loading="lazy" src="https://bio.libretexts.org/@api/deki/files/6296/ATP_synthase.png?revision=1" /><figcaption>Figure <mjx-container class="MathJax CtxtMenu_Attached_0" jax="SVG" overflow="linebreak" tabindex="0" ctxtmenu_counter="96" style="font-size: 85%; position: relative;"><svg width="4.652ex" height="1.581ex" role="img" focusable="false" viewbox="0 -677 2056 699" aria-hidden="true" style="vertical-align: -0.05ex;"><defs><path id="MJX-97-NCM-N-34" d="M353 677C344 677 336 672 330 663L28 199L28 163L289 163L289 81C289 63 285 51 278 46C271 41 252 39 219 39L194 39L194 0C223 2 269 3 331 3C393 3 439 2 468 0L468 39L443 39C410 39 391 41 384 46C377 51 373 63 373 81L373 163L471 163L471 202L373 202L373 660C373 670 366 677 353 677M295 553L295 202L67 202Z"></path><path id="MJX-97-NCM-N-2E" d="M192 53C192 82 168 106 139 106C110 106 86 82 86 53C86 24 110 0 139 0C168 0 192 24 192 53Z"></path><path id="MJX-97-NCM-N-36" d="M383 504C416 504 432 521 432 555C432 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<p class="lt-bio-4632" style="background-color: unset;">ATP synthase can be separated into 2 parts:</p>

<ul>
    <li class="lt-bio-4632" style="background-color: unset;">F<sub><font size="2">o</font></sub> - the portion embedded in the inner mitochondrial membrane</li>
    <li class="lt-bio-4632" style="background-color: unset;">F<sub><small><font size="1">1</font></small></sub>-ATPase &mdash; the portion projecting into the matrix of the mitochondrion</li>
</ul>

<p class="lt-bio-4632" style="background-color: unset;">This is why the intact ATP synthase is also called the F<sub><font size="2">o</font></sub>F<sub><small><font size="1">1</font></small></sub>-ATPase.</p>

<p class="lt-bio-4632" style="background-color: unset;">When the F<sub><small><font size="1">1</font></small></sub>-ATPase is isolated in vitro, it catalyzes the hydrolysis of ATP to ADP and P<sub><font size="2">i</font></sub> (which is why it is called the F<sub><small><font size="1">1</font></small></sub>-ATPase). While it is doing so, the central portion of F<sub><font size="2">o</font></sub> attached to the stalk rotates rapidly in a counter-clockwise direction (as viewed from above).</p>

<p class="lt-bio-4632" style="background-color: unset;">In the intact mitochondrion, the protons that have accumulated in the intermembrane space enter the F<sub><font size="2">o</font></sub> complex and exit from it into the matrix. The energy they give up as they travel down their concentration gradient rotates F<sub><font size="2">o</font></sub> and its stalk (at ~6000 rpm) in a clockwise direction. As it does so, it induces repeating conformational changes in the head proteins that enable them to convert ADP and P<sub><font size="2">i</font></sub> into ATP. (In the figure, two of the three dimers that make up the head proteins have been pulled aside to reveal the stalk inserted in their center.)</p>

<p class="lt-bio-4632" style="background-color: unset;">In both these cases, the machine is converting chemical energy from the hydrolysis of ATP in the in vitro case and the flow of protons down their concentration gradient in the intact mitochondrion into mechanical energy &mdash; the turning of the motor. But this remarkable device can be made to do the reverse, converting mechanical energy (turning of the motor) into chemical energy.</p>

<div class="box-note">
<p class="lt-bio-4632" style="background-color: unset;">A group of Japanese scientists interested in nano-machines have succeeded in attaching magnetic beads to the stalks of the F<sub><small><font size="1">1</font></small></sub>-ATPase isolated <em>in vitro</em>. Then using a rotating magnetic field they were able to make the stalks rotate. When rotated in a clockwise direction, the F<sub><small><font size="1">1</font></small></sub>-ATPase synthesized ATP from ADP and P<sub><font size="2">i</font></sub> in the surrounding medium &mdash; at a rate of about 5 molecules per second! (When rotating the stalks in the counter-clockwise direction, or not rotating them at all, ATP was hydrolyzed into ADP and P<sub><font size="2">i</font></sub>.)</p>

<p class="lt-bio-4632" style="background-color: unset;">Their achievement was reported in Itoh, H., <em>et al</em>., <strong>Nature</strong>, 29 January 2004.</p>
</div>

<span id="Contributors_and_Attributions"></span><span id="Contributors_and_Attributions"></span><h2 style="background-color: unset;" class="lt-bio-4632">Contributors and Attributions</h2>

<ul>
    <li class="lt-bio-4632" style="background-color: unset;"><p style="text-align: justify;"><a title="http://www.biology-pages.info/" href="http://www.biology-pages.info/" target="_blank" rel="external noopener nofollow" class="external">John W. Kimball</a>. This content is distributed under a Creative Commons Attribution 3.0 Unported (CC BY 3.0) license and made possible by funding from <a title="http://www.saylor.org" href="http://www.saylor.org" target="_blank" rel="external noopener nofollow" class="external">The Saylor Foundation.</a></p>

</li>
</ul>

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<hr class="autoattribution-divider" /><div class="autoattribution"><p>This page titled <a target="_blank" class="internal mt-self-link" href="/Sandboxes/johnnyphung/biology/04:_Cell_Metabolism/4.06:_ATP_Synthase">4.6: ATP Synthase</a> is shared under a <a rel="nofollow" href="https://creativecommons.org/licenses/by/3.0" target="_blank">CC BY  3.0</a>  license and was authored, remixed, and/or curated by <a rel="nofollow" target="_blank" href="http://www.biology-pages.info/">John W. Kimball</a> via <a rel="nofollow" href="https://www.biology-pages.info/" target="_blank">source content</a> that was edited to the style and standards of the LibreTexts platform.</p></div>

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