Difference between revisions of "Gnaiger 2023 MitoFit CII"
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The current narrative that the reduced coenzymes NADH and FADH<sub>2</sub> feed electrons from the tricarboxylic acid cycle into the mitochondrial electron transfer system creates ambiguities around respiratory Complex II (CII). The succinate dehydrogenase subunit SDHA of CII oxidizes succinate and reduces covalently bound FAD to FADH<sub>2</sub> in the canonical forward tricarboxylic acid cycle. However, several graphical representations of the membrane-bound electron transfer system (ETS) depict FADH<sub>2</sub> in the mitochondrial matrix to be oxidized by CII. This leads to the false conclusion that FADH<sub>2</sub> feeds electrons into the ETS through CII, including FADH<sub>2</sub> from the tricarboxylic acid cycle, the Ī²-oxidation cycle in fatty acid oxidation, and the glycerophosphate shuttle. In reality, FAD and succinate are the ''substrates'' of SDHA at the ETS-entry into CII. The reduced flavin groups FADH<sub>2</sub> and FMNH<sub>2</sub> are ''products'' downstream within CII and CI, respectively. Further electron transfer converges at the coenzyme Q-junction. Similarly, electron transferring flavoprotein and mitochondrial glycerophosphate dehydrogenase feed electrons into the Q-junction but not through CII. The ambiguities surrounding Complex II in the literature and educational tools call for quality control, to secure scientific standards in current communications on bioenergetics and ultimately support adequate clinical applications. | The current narrative that the reduced coenzymes NADH and FADH<sub>2</sub> feed electrons from the tricarboxylic acid cycle into the mitochondrial electron transfer system creates ambiguities around respiratory Complex II (CII). The succinate dehydrogenase subunit SDHA of CII oxidizes succinate and reduces covalently bound FAD to FADH<sub>2</sub> in the canonical forward tricarboxylic acid cycle. However, several graphical representations of the membrane-bound electron transfer system (ETS) depict FADH<sub>2</sub> in the mitochondrial matrix to be oxidized by CII. This leads to the false conclusion that FADH<sub>2</sub> feeds electrons into the ETS through CII, including FADH<sub>2</sub> from the tricarboxylic acid cycle, the Ī²-oxidation cycle in fatty acid oxidation, and the glycerophosphate shuttle. In reality, FAD and succinate are the ''substrates'' of SDHA at the ETS-entry into CII. The reduced flavin groups FADH<sub>2</sub> and FMNH<sub>2</sub> are ''products'' downstream within CII and CI, respectively. Further electron transfer converges at the coenzyme Q-junction. Similarly, electron transferring flavoprotein and mitochondrial glycerophosphate dehydrogenase feed electrons into the Q-junction but not through CII. The ambiguities surrounding Complex II in the literature and educational tools call for quality control, to secure scientific standards in current communications on bioenergetics and ultimately support adequate clinical applications. | ||
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|keywords=coenzyme Q junction; Complex CII; electron transfer system; fatty acid oxidation; flavin adenine dinucleotide; | |keywords=coenzyme Q junction; Complex CII; electron transfer system; fatty acid oxidation; flavin adenine dinucleotide;succinate dehydrogenase; tricarboxylic acid cycle | ||
succinate dehydrogenase; tricarboxylic acid cycle | |||
|mipnetlab=AT Innsbruck Oroboros | |mipnetlab=AT Innsbruck Oroboros | ||
}} | }} | ||
Ā | {{Labeling | ||
|additional=FAT4BRAIN, Publication:FAT4BRAIN | |||
}} | |||
[[File:N-S FADH2-FMNH2.png|right|600px]] | [[File:N-S FADH2-FMNH2.png|right|600px]] | ||
:::: '''Figure 1. Complex II bridges electron transfer from the TCA cycle to the mitochondrial inner membrane'''. Graphical representations of the electron transfer system ETS with successive emphasis on pathway architecture and concomitant loss of detail. CII is integrated in the TCA cycle (matrix-ETS) and the membrane-bound electron transfer system (membrane-ETS in the mt-inner membrane mtIM). Joint half-circular arrows indicate electron transfer 2{H<sup>+</sup>+eĀ<sup>-</sup>}, distinguished from hydrogen ion H<sup>+</sup> transport across the mtIM. '''(a)''' In the soluble domain of CII, the flavoprotein SDHA catalyzes the oxidation succinate ā fumarate+2{H<sup>+</sup>+e<sup>-</sup>} and reduction FAD+2{H<sup>+</sup>+e<sup>-</sup>} ā FADH<sub>2</sub>. The ironāsulfur protein SDHB transfers electrons through Fe-S clusters to the mtIM domain where ubiquinone UQ is reduced with 2{H<sup>+</sup>+e<sup>-</sup>} to ubiquinol UQH<sub>2</sub> in SDHC and SDHD. '''(b)''' NADH and succinate are substrates of redox reactions in CI and CII, respectively, with FMNH<sub>2</sub> and FADH<sub>2</sub> as the corresponding products. Succinate and fumarate indicate the chemical entities irrespective of ionization, whereas the charges are shown in NADH, NAD<sup>+</sup>, and H<sup>+</sup>. '''(c)''' Electron flow catalyzed by dehydrognases localized in the mitochondrial (mt) matrix converges at the N-junction, reducing NAD<sup>+</sup> to NADH. Electron flow from NADH and succinate S to molecular oxygen, 2{H<sup>+</sup>+e<sup>-</sup>}+0.5 O<sub>2</sub> ā¢ H<sub>2</sub>O, converges through CI and CII at the Q-junction. CIII passes electrons to cytochrome ''c'' and in CIV to O<sub>2</sub>. Ā | :::: '''Figure 1. Complex II bridges electron transfer from the TCA cycle to the mitochondrial inner membrane'''. Graphical representations of the electron transfer system ETS with successive emphasis on pathway architecture and concomitant loss of detail. CII is integrated in the TCA cycle (matrix-ETS) and the membrane-bound electron transfer system (membrane-ETS in the mt-inner membrane mtIM). Joint half-circular arrows indicate electron transfer 2{H<sup>+</sup>+eĀ<sup>-</sup>}, distinguished from hydrogen ion H<sup>+</sup> transport across the mtIM. '''(a)''' In the soluble domain of CII, the flavoprotein SDHA catalyzes the oxidation succinate ā fumarate+2{H<sup>+</sup>+e<sup>-</sup>} and reduction FAD+2{H<sup>+</sup>+e<sup>-</sup>} ā FADH<sub>2</sub>. The ironāsulfur protein SDHB transfers electrons through Fe-S clusters to the mtIM domain where ubiquinone UQ is reduced with 2{H<sup>+</sup>+e<sup>-</sup>} to ubiquinol UQH<sub>2</sub> in SDHC and SDHD. '''(b)''' NADH and succinate are substrates of redox reactions in CI and CII, respectively, with FMNH<sub>2</sub> and FADH<sub>2</sub> as the corresponding products. Succinate and fumarate indicate the chemical entities irrespective of ionization, whereas the charges are shown in NADH, NAD<sup>+</sup>, and H<sup>+</sup>. '''(c)''' Electron flow catalyzed by dehydrognases localized in the mitochondrial (mt) matrix converges at the N-junction, reducing NAD<sup>+</sup> to NADH. Electron flow from NADH and succinate S to molecular oxygen, 2{H<sup>+</sup>+e<sup>-</sup>}+0.5 O<sub>2</sub> ā¢ H<sub>2</sub>O, converges through CI and CII at the Q-junction. CIII passes electrons to cytochrome ''c'' and in CIV to O<sub>2</sub>. Ā | ||
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:::::: [[File:Expii-Gabi Slizewska CORRECTION.png|400px]] | :::::: [[File:Expii-Gabi Slizewska CORRECTION.png|400px]] | ||
:::: '''Website 9''': [https://www.expii.com/t/electron-transport-chain-summary-diagrams-10139 expii] - Image source: By Gabi Slizewska | :::: '''Website 9''': [https://www.expii.com/t/electron-transport-chain-summary-diagrams-10139 expii] - Image source: By Gabi Slizewska | ||
Revision as of 12:06, 17 April 2023
Gnaiger E (2023) Complex II ambiguities ā FADH2 in the electron transfer system. MitoFit Preprints 2023.3.v2. https://doi.org/10.26124/mitofit:2023-0003.v2 |
Ā» MitoFit Preprints 2023.3.v2.
Complex II ambiguities ā FADH2 in the electron transfer system
Gnaiger Erich (2023) MitoFit Prep
Abstract:
- Version 2 (v2) 2023-04-04 10.26124/mitofit:2023-0003.v2
- Version 1 (v1) 2023-03-247 10.26124/mitofit:2023-0003 - Ā»Link to all versionsĀ«
The current narrative that the reduced coenzymes NADH and FADH2 feed electrons from the tricarboxylic acid cycle into the mitochondrial electron transfer system creates ambiguities around respiratory Complex II (CII). The succinate dehydrogenase subunit SDHA of CII oxidizes succinate and reduces covalently bound FAD to FADH2 in the canonical forward tricarboxylic acid cycle. However, several graphical representations of the membrane-bound electron transfer system (ETS) depict FADH2 in the mitochondrial matrix to be oxidized by CII. This leads to the false conclusion that FADH2 feeds electrons into the ETS through CII, including FADH2 from the tricarboxylic acid cycle, the Ī²-oxidation cycle in fatty acid oxidation, and the glycerophosphate shuttle. In reality, FAD and succinate are the substrates of SDHA at the ETS-entry into CII. The reduced flavin groups FADH2 and FMNH2 are products downstream within CII and CI, respectively. Further electron transfer converges at the coenzyme Q-junction. Similarly, electron transferring flavoprotein and mitochondrial glycerophosphate dehydrogenase feed electrons into the Q-junction but not through CII. The ambiguities surrounding Complex II in the literature and educational tools call for quality control, to secure scientific standards in current communications on bioenergetics and ultimately support adequate clinical applications.
ā¢ Keywords: coenzyme Q junction; Complex CII; electron transfer system; fatty acid oxidation; flavin adenine dinucleotide;succinate dehydrogenase; tricarboxylic acid cycle
ā¢ O2k-Network Lab: AT Innsbruck Oroboros
Labels:
FAT4BRAIN, Publication:FAT4BRAIN
- Figure 1. Complex II bridges electron transfer from the TCA cycle to the mitochondrial inner membrane. Graphical representations of the electron transfer system ETS with successive emphasis on pathway architecture and concomitant loss of detail. CII is integrated in the TCA cycle (matrix-ETS) and the membrane-bound electron transfer system (membrane-ETS in the mt-inner membrane mtIM). Joint half-circular arrows indicate electron transfer 2{H++eĀ-}, distinguished from hydrogen ion H+ transport across the mtIM. (a) In the soluble domain of CII, the flavoprotein SDHA catalyzes the oxidation succinate ā fumarate+2{H++e-} and reduction FAD+2{H++e-} ā FADH2. The ironāsulfur protein SDHB transfers electrons through Fe-S clusters to the mtIM domain where ubiquinone UQ is reduced with 2{H++e-} to ubiquinol UQH2 in SDHC and SDHD. (b) NADH and succinate are substrates of redox reactions in CI and CII, respectively, with FMNH2 and FADH2 as the corresponding products. Succinate and fumarate indicate the chemical entities irrespective of ionization, whereas the charges are shown in NADH, NAD+, and H+. (c) Electron flow catalyzed by dehydrognases localized in the mitochondrial (mt) matrix converges at the N-junction, reducing NAD+ to NADH. Electron flow from NADH and succinate S to molecular oxygen, 2{H++e-}+0.5 O2 ā¢ H2O, converges through CI and CII at the Q-junction. CIII passes electrons to cytochrome c and in CIV to O2.
ORCID: Gnaiger Erich, Oroboros Instruments, Innsbruck, Austria
- Acknowledgements: I thank Luiza H. Cardoso and Sabine Schmitt for stimulating discussions, and Paolo Cocco for expert help on the graphical abstract and Figures 1b and c. Contribution to the European Unionās Horizon 2020 research and innovation program Grant 857394 (FAT4BRAIN).
Updates to Supplement Figure S1
Last update 2023-04-15
- Figure S1. Complex II ambiguities in graphical representations on FADH2 as a substrate of Complex II in the canonical forward electron transfer. Chronological sequence of publications from 2001 to 2023.
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Supplement Figure S1 (v2)
- Figure S1. Complex II ambiguities in graphical representations on FADH2 as a substrate of Complex II in the canonical forward electron transfer. Chronological sequence of publications from 2001 to 2023.
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Supplement Figure S2 (v2)
- Figure S2. Complex II ambiguities in graphical representations on FADH2 as a substrate of Complex II in the canonical forward electron transfer (retrieved 2023-03-21 to 2023-04-04)
- Website 1: OpenStax Biology - Fig. 7.10 Oxidative phosphorylation (CC BY 3.0). - OpenStax Biology got it wrong in figures and text. The error is copied without quality assessment and propagated in several links.
- Website 2: Concepts of Biology - 1st Canadian Edition by Charles Molnar and Jane Gair - Fig. 4.19a
- Website 3: LibreTexts Biology Oxidative Phosphorylation - Electron Transport Chain - Figure 7.11.1
- Website 4: lumen Biology for Majors I - Fig. 1
- Website 5: Pharmaguideline
- Website 37: Texas Gateway - Figure 7.11
- Website 38: Concepts of Biology - Charles Molnar and Jane Gair. 4.3 Citric Acid Cycle and Oxidative Phosphorylation. Concepts of Biology - 1st Canadian Edition, BCcampus
- Website 39: -CUNY
- Website 40: - Brain Brooder
- Website 6: Khan Academy - Image modified from "Oxidative phosphorylation: Figure 1", by OpenStax College, Biology (CC BY 3.0). Figure and text underscore the FADH2-error: "FADH2 .. feeds them (electrons) into the transport chain through complex II."
- Website 7: Saylor Academy
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- Website 1: OpenStax Biology - Fig. 7.12
- Website 6: Khan Academy - Image modified from "Oxidative phosphorylation: Figure 3," by Openstax College, Biology (CC BY 3.0)
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- Website 9: expii - Image source: By CNX OpenStax
- Website 37: Texas Gateway - Figure 7.11
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- Website 10: Labxchange - Figure 8.15 credit: modification of work by Klaus Hoffmeier
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- Website 9: expii - By OpenStax College CC BY 3.0, via Wikimedia Commons
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