https://wiki.oroboros.at/index.php?title=F-junction&feed=atom&action=historyF-junction - Revision history2024-03-28T14:08:05ZRevision history for this page on the wikiMediaWiki 1.36.1https://wiki.oroboros.at/index.php?title=F-junction&diff=223954&oldid=prevCecatto Cristiane at 15:06, 18 January 20222022-01-18T15:06:10Z<p></p>
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</table>Cecatto Cristianehttps://wiki.oroboros.at/index.php?title=F-junction&diff=212213&oldid=prevGnaiger Erich at 18:10, 1 January 20212021-01-01T18:10:28Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer pathway]] (ET-pathway) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer pathway]] (ET-pathway) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger <del style="font-weight: bold; text-decoration: none;">2014 </del>MitoPathways]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger <ins style="font-weight: bold; text-decoration: none;">2020 BEC </ins>MitoPathways]]</div></td></tr>
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</table>Gnaiger Erichhttps://wiki.oroboros.at/index.php?title=F-junction&diff=203381&oldid=prevBeno Marija at 12:20, 8 June 20202020-06-08T12:20:32Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer<del style="font-weight: bold; text-decoration: none;">-</del>pathway]] (ET-pathway) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer pathway]] (ET-pathway) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td></tr>
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</table>Beno Marijahttps://wiki.oroboros.at/index.php?title=F-junction&diff=144429&oldid=prevBeno Marija at 13:32, 20 October 20172017-10-20T13:32:30Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer <del style="font-weight: bold; text-decoration: none;">system</del>]] (ET-pathway) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer<ins style="font-weight: bold; text-decoration: none;">-pathway</ins>]] (ET-pathway) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
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</table>Beno Marijahttps://wiki.oroboros.at/index.php?title=F-junction&diff=144267&oldid=prevBeno Marija at 11:47, 20 October 20172017-10-20T11:47:49Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (<del style="font-weight: bold; text-decoration: none;">ETS</del>) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (<ins style="font-weight: bold; text-decoration: none;">ET-pathway</ins>) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation, in the [[F-pathway control state]], not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td></tr>
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</table>Beno Marijahttps://wiki.oroboros.at/index.php?title=F-junction&diff=124569&oldid=prevGnaiger Erich at 10:43, 8 November 20162016-11-08T10:43:49Z<p></p>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids <del style="font-weight: bold; text-decoration: none;">([[ETS substrate types |F-junction substrates]]) </del>through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation <del style="font-weight: bold; text-decoration: none;">(</del>the [[<del style="font-weight: bold; text-decoration: none;">FAO</del>]] <del style="font-weight: bold; text-decoration: none;">substrate state) </del>not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation<ins style="font-weight: bold; text-decoration: none;">, in </ins>the [[<ins style="font-weight: bold; text-decoration: none;">F-pathway control state</ins>]]<ins style="font-weight: bold; text-decoration: none;">, </ins>not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N-junction substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">Contributed </del>by [[Gnaiger E]] 2016-02-12</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div><ins style="font-weight: bold; text-decoration: none;"> Communicated </ins>by [[Gnaiger E]] 2016-02-12<ins style="font-weight: bold; text-decoration: none;">, edited 2016-11-08.</ins></div></td></tr>
</table>Gnaiger Erichhttps://wiki.oroboros.at/index.php?title=F-junction&diff=119774&oldid=prevGnaiger Erich at 05:37, 10 September 20162016-09-10T05:37:12Z<p></p>
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 05:37, 10 September 2016</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-catg F.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |<del style="font-weight: bold; text-decoration: none;">type </del>F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the <del style="font-weight: bold; text-decoration: none;">type </del>N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |F<ins style="font-weight: bold; text-decoration: none;">-junction </ins>substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the N<ins style="font-weight: bold; text-decoration: none;">-junction </ins>substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
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</table>Gnaiger Erichhttps://wiki.oroboros.at/index.php?title=F-junction&diff=118169&oldid=prevGnaiger Erich at 21:36, 21 August 20162016-08-21T21:36:41Z<p></p>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-<del style="font-weight: bold; text-decoration: none;">Catg NF</del>.jpg|right|300px|F-junction]]</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-<ins style="font-weight: bold; text-decoration: none;">catg F</ins>.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |type F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the type N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |type F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the type N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCoA inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCoA into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td></tr>
</table>Gnaiger Erichhttps://wiki.oroboros.at/index.php?title=F-junction&diff=118088&oldid=prevGnaiger Erich at 09:49, 19 August 20162016-08-19T09:49:30Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 09:49, 19 August 2016</td>
</tr><tr><td colspan="2" class="diff-lineno" id="mw-diff-left-l1">Line 1:</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{MitoPedia</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>{{MitoPedia</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-Catg NF.jpg|right|300px|F-junction]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|description=[[File:SUIT-Catg NF.jpg|right|300px|F-junction]]</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |type F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the type N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of <del style="font-weight: bold; text-decoration: none;">AcetylCo </del>inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of <del style="font-weight: bold; text-decoration: none;">AcetylCo </del>into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |type F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the type N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of <ins style="font-weight: bold; text-decoration: none;">AcetylCoA </ins>inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of <ins style="font-weight: bold; text-decoration: none;">AcetylCoA </ins>into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">{{MitoPedia O2k and high-resolution respirometry}}</del></div></td><td colspan="2"></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;">{{MitoPedia topics}}</del></div></td><td colspan="2"></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Contributed by [[Gnaiger E]] 2016-02-12</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>Contributed by [[Gnaiger E]] 2016-02-12</div></td></tr>
</table>Gnaiger Erichhttps://wiki.oroboros.at/index.php?title=F-junction&diff=111590&oldid=prevPlattner Christina at 14:41, 13 May 20162016-05-13T14:41:26Z<p></p>
<table style="background-color: #fff; color: #202122;" data-mw="interface">
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<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">← Older revision</td>
<td colspan="2" style="background-color: #fff; color: #202122; text-align: center;">Revision as of 14:41, 13 May 2016</td>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |type F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the type N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCo inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCo into the TCA cycle catalyzed by citrate synthase.</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>The '''F-junction''' is a junction for [[convergent electron flow]] in the [[electron transfer system]] (ETS) from fatty acids ([[ETS substrate types |type F substrates]]) through [[fatty acyl CoA dehydrogenase]] (reduced form [[FADH2]]) to [[electron transferring flavoprotein]] (CETF), and further transfer through the [[Q-junction]] to [[Complex III]] (CIII). The concept of the F-junction and [[N-junction]] provides a basis for defining [[categories of SUIT protocols]]. Fatty acid oxidation (the [[FAO]] substrate state) not only depends on electron transfer through the F-junction (which is typically rate-limiting) but simultaneously generates NADH and thus depends on N-junction throughput. Hence FAO can be inhibited completely by inhibition of Complex I (CI). In addition and independent of this source of NADH, the type N substrate malate is required as a co-substrate for FAO in mt-preparations, since accumulation of AcetylCo inhibits FAO in the absence of malate. Malate is oxidized in a reaction catalyzed by malate dehydrogenase to oxaloacetate (yielding NADH), which then stimulates the entry of AcetylCo into the TCA cycle catalyzed by citrate synthase.</div></td></tr>
<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|info=[[Gnaiger 2014 MitoPathways]]</div></td></tr>
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<tr><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mitopedia method=Respirometry</div></td><td class="diff-marker"></td><td style="background-color: #f8f9fa; color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #eaecf0; vertical-align: top; white-space: pre-wrap;"><div>|mitopedia method=Respirometry</div></td></tr>
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<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div>}}</div></td><td class="diff-marker" data-marker="+"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #a3d3ff; vertical-align: top; white-space: pre-wrap;"><div>Contributed by [[Gnaiger E]] 2016-02-12</div></td></tr>
<tr><td class="diff-marker" data-marker="−"></td><td style="color: #202122; font-size: 88%; border-style: solid; border-width: 1px 1px 1px 4px; border-radius: 0.33em; border-color: #ffe49c; vertical-align: top; white-space: pre-wrap;"><div><del style="font-weight: bold; text-decoration: none;"> </del>Contributed by [[Gnaiger E]] 2016-02-12</div></td><td colspan="2"></td></tr>
</table>Plattner Christina