Krebs cycle step 6: Difference between revisions

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<h2>Step 6 of the Krebs cycle: Succinate Dehydrogenase</h2>
<h2>Step 6 of the Krebs cycle: [[Succinate Dehydrogenase]]</h2>
[[Image:succinat_2.jpg]]
[[Image:succinat_2.jpg]]
<p>Figure: Formation of Fumarate</p>
<p>Figure: Formation of Fumarate</p>


<p>In the sixth step, succinate is converted to fumarate; here, a dehydrogenation takes place because two protons are removed. FAD serves as coenzyme wich is bound covalently to the enzyme succinate dehydrogenase, so that usually the notation E-FAD is used.  The liberated protons (in yellow) are taken up by FAD which is oxidised to FADH<sub>2</sub>. Unlike NADH, FADH<sub>2</sub> does not need to be  
<p>In the sixth step, succinate is converted to fumarate; here, a dehydrogenation takes place because two protons are removed. FAD serves as coenzyme wich is bound covalently to the enzyme succinate dehydrogenase, so that usually the notation E-FAD is used.  The liberated protons (in yellow) are taken up by FAD which is oxidised to FADH<sub>2</sub>. Unlike NADH, FADH<sub>2</sub> does not need to be  
funneled into the respiratory chain, but is reduced directly in the enzyme back to FAD, and the reaciton can take place with another succinate molecule. </p>
funneled into the respiratory chain, but is reduced directly in the enzyme back to FAD, and the reaciton can take place with another succinate molecule. </p>

Latest revision as of 12:37, 18 December 2019

Step 6 of the Krebs cycle: Succinate Dehydrogenase

Figure: Formation of Fumarate

In the sixth step, succinate is converted to fumarate; here, a dehydrogenation takes place because two protons are removed. FAD serves as coenzyme wich is bound covalently to the enzyme succinate dehydrogenase, so that usually the notation E-FAD is used. The liberated protons (in yellow) are taken up by FAD which is oxidised to FADH2. Unlike NADH, FADH2 does not need to be funneled into the respiratory chain, but is reduced directly in the enzyme back to FAD, and the reaciton can take place with another succinate molecule.

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Verena Pietzner, Jaime Prilusky, Alexander Berchansky