Electron Transport & Oxidative Phosphorylation: Difference between revisions
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<StructureSection load='2f1o.pdb' size='350' frame='true' side='right' scene='2f1o/Com_view/2' caption='NADPH dehydrogenase complex with FAD and dicoumarol [[2f1o]]'> | <StructureSection load='2f1o.pdb' size='350' frame='true' side='right' scene='2f1o/Com_view/2' caption='NADPH dehydrogenase complex with FAD and dicoumarol [[2f1o]]'> | ||
[[Electron Transport & Oxidative Phosphorylation]] is a metabolic pathway that uses the energy released from the [[Citric Acid Cycle]] and oxygen to produce ATP. It is the major ATP production mechanism in human [[carbohydrate metabolism]]. | [[Electron Transport & Oxidative Phosphorylation]] is a metabolic pathway that uses the energy released from the [[Citric Acid Cycle]] and oxygen to produce ATP. It is the major ATP production mechanism in human [[carbohydrate metabolism]]. See also [https://en.wikipedia.org/wiki/Oxidative_phosphorylation]. | ||
'''NADH-coenzyme Q oxidoreductase (complex I)''' | '''NADH-coenzyme Q oxidoreductase (complex I)''' | ||
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The start of the reaction, and indeed of the entire electron chain, is the binding of a NADH molecule to complex I and the donation of two electrons. The electrons enter complex I via a prosthetic group attached to the complex, <scene name='43/430899/Cv/3'>flavin mononucleotide</scene> (FMN). The addition of electrons to FMN converts it to its reduced form, FMNH2. The electrons are then transferred through a series of iron–sulfur clusters: the second kind of prosthetic group present in the complex. There are both [2Fe–2S] and [4Fe–4S] iron–sulfur clusters in complex I. | The start of the reaction, and indeed of the entire electron chain, is the binding of a NADH molecule to complex I and the donation of two electrons. The electrons enter complex I via a prosthetic group attached to the complex, <scene name='43/430899/Cv/3'>flavin mononucleotide</scene> (FMN). The addition of electrons to FMN converts it to its reduced form, FMNH2. The electrons are then transferred through a series of iron–sulfur clusters: the second kind of prosthetic group present in the complex. There are both [2Fe–2S] and [4Fe–4S] iron–sulfur clusters in complex I. | ||
'''Complex III''' | '''Succinate-Q oxidoreductase (complex II)''' | ||
*[[Succinate Dehydrogenase]] | |||
Succinate-Q oxidoreductase, also known as complex II or succinate dehydrogenase, is a second entry point to the electron transport chain. It is unusual because it is the only enzyme that is part of both the citric acid cycle and the electron transport chain. Complex II consists of four protein subunits and contains a bound <scene name='43/430899/Cv/4'>flavin adenine dinucleotide</scene> (FAD) cofactor, iron–sulfur clusters, and a heme group that does not participate in electron transfer to coenzyme Q, but is believed to be important in decreasing production of reactive oxygen species. | |||
<scene name='43/430893/Cv/10'>Succinate</scene> + Q -> <scene name='43/430893/Cv/11'>Fumarate</scene> + QH2 | |||
'''Q-cytochrome c oxidoreductase (complex III)''' | |||
* [[Complex III of Electron Transport Chain]] | * [[Complex III of Electron Transport Chain]] | ||
* [[Cytochrome bc1 complex]] | |||
* [[Cytochrome b]] | |||
The reaction catalyzed by complex III is the oxidation of one molecule of ubiquinol and the reduction of two molecules of cytochrome c, a heme protein loosely associated with the mitochondrion. Unlike coenzyme Q, which carries two electrons, cytochrome c carries only one electron. | |||
QH<sub>2</sub>+ 2 Cyt c<sub>ox</sub> + 2H<sup>+</sup>(matrix) -> Q + 2 Cyt c<sub>red</sub> + 4H<sup>+</sup>(intermembrane) | |||
'''Cytochrome c oxidase (complex IV)''' | |||
*[[Cytochrome c oxidase]] | |||
Cytochrome c oxidase, also known as complex IV, is the final protein complex in the electron transport chain. The mammalian enzyme has an extremely complicated structure and contains <scene name='46/466466/Cv/9'>13 subunits</scene>, two <scene name='46/466466/Cv/10'>heme groups, as well as multiple metal ion cofactors – in all, three atoms of copper, one of magnesium and one of zinc</scene>. The fully oxidized form of <scene name='46/466466/Cv/11'>CcO active site shows the heme, Cu+2 ion and an O2</scene> molecule. <scene name='46/466466/Cv/12'>Second heme binding site</scene>. <ref>PMID:9624044</ref> Bacterial CcO is composed of 2 subunits. | |||
4Cyt c<sub>red</sub> +O<sub>2</sub> + 8H<sup>+</sup>(matrix) -> 4Cyt c<sub>ox</sub> + 2H<sub>2</sub>O +4H<sup>+</sup>(intermembrane) | |||
</StructureSection> | </StructureSection> | ||
== References == | |||
<references/> | |||