Gnaiger 2023 MitoFit CII: Difference between revisions

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{{Publication
{{Publication
|title=Gnaiger E (2023) Complex II ambiguities ― FADH<sub>2</sub> in the electron transfer system. MitoFit Preprints 2023.3.v6. https://doi.org/10.26124/mitofit:2023-0003.v6
|title=Gnaiger E (2023) Complex II ambiguities ― FADH<sub>2</sub> in the electron transfer system. MitoFit Preprints 2023.3.v6. https://doi.org/10.26124/mitofit:2023-0003.v6 - ''' [[Gnaiger 2024 J Biol Chem |''Published 2023-11-22 J Biol Chem (2024)'']]
|info=MitoFit Preprints 2023.3.v6. [[File:MitoFit Preprints pdf.png|left|160px|link=https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf|MitoFit pdf]] [https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf Complex II ambiguities ― FADH<sub>2</sub> in the electron transfer system]<br/>
|info=MitoFit Preprints 2023.3.v6. [[File:MitoFit Preprints pdf.png|left|160px|link=https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf|MitoFit pdf]] [https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf Complex II ambiguities ― FADH<sub>2</sub> in the electron transfer system]<br/>
|authors=Gnaiger Erich
|authors=Gnaiger Erich
|year=2023
|year=2023
|journal=MitoFit Prep
|journal=MitoFit Prep
|abstract=[[File:CII-ambiguities Graphical abstract.png|200px|left]]
|abstract=[[File:CII-ambiguities Graphical abstract.png|150px|left]]
::: '''Version 6 (v6) 2023-06-21''' [https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf 10.26124/mitofit:2023-0003.v6]
::: Gnaiger E (2024) Complex II ambiguities ― FADH<sub>2</sub> in the electron transfer system. J Biol Chem 300:105470. https://doi.org/10.1016/j.jbc.2023.105470
::: <small>Version 5 (v5) 2023-05-31 </small>
::: <small>Version 6 (v6) 2023-06-21 </small>
::: <small>Version 4 (v4) 2023-05-12 </small>
::: <small>Version 5 (v5) 2023-05-31, (v4) 2023-05-12, (v3) 2023-05-04, (v2) 2023-04-04, (v1) 2023-03-24 - [https://wiki.oroboros.at/index.php/File:Gnaiger_2023_MitoFit_CII.pdf »Link to all versions«]</small>
::: <small>Version 3 (v3) 2023-05-04 </small>
::: <small>Version 2 (v2) 2023-04-04 </small>
::: <small>Version 1 (v1) 2023-03-24 - [https://wiki.oroboros.at/index.php/File:Gnaiger_2023_MitoFit_CII.pdf »Link to all versions«]</small>
The prevailing notion that reduced cofactors NADH and FADH<sub>2</sub> transfer electrons from the tricarboxylic acid cycle to the mitochondrial electron transfer system creates ambiguities regarding respiratory Complex II (CII). The succinate dehydrogenase subunit SDHA of CII oxidizes succinate and reduces the covalently bound prosthetic group FAD to FADH<sub>2</sub> in the canonical forward tricarboxylic acid cycle. However, several graphical representations of the electron transfer system depict FADH<sub>2</sub> in the mitochondrial matrix as a substrate to be oxidized by CII. This leads to the false conclusion that FADH<sub>2</sub> from the β-oxidation cycle in fatty acid oxidation feeds electrons into CII. In reality, dehydrogenases of fatty acid oxidation channel electrons to the coenzyme Q-junction but not through CII. The ambiguities surrounding Complex II in the literature and educational resources call for quality control, to secure scientific standards in current communications of bioenergetics, and ultimately support adequate clinical applications. This review aims to raise awareness of the inherent '''[[ambiguity crisis]]''', complementing efforts to address the well-acknowledged issues of credibility and reproducibility.
The prevailing notion that reduced cofactors NADH and FADH<sub>2</sub> transfer electrons from the tricarboxylic acid cycle to the mitochondrial electron transfer system creates ambiguities regarding respiratory Complex II (CII). The succinate dehydrogenase subunit SDHA of CII oxidizes succinate and reduces the covalently bound prosthetic group FAD to FADH<sub>2</sub> in the canonical forward tricarboxylic acid cycle. However, several graphical representations of the electron transfer system depict FADH<sub>2</sub> in the mitochondrial matrix as a substrate to be oxidized by CII. This leads to the false conclusion that FADH<sub>2</sub> from the β-oxidation cycle in fatty acid oxidation feeds electrons into CII. In reality, dehydrogenases of fatty acid oxidation channel electrons to the coenzyme Q-junction but not through CII. The ambiguities surrounding Complex II in the literature and educational resources call for quality control, to secure scientific standards in current communications of bioenergetics, and ultimately support adequate clinical applications. This review aims to raise awareness of the inherent '''[[ambiguity crisis]]''', complementing efforts to address the well-acknowledged issues of credibility and reproducibility.
<br>
<br>
|keywords=coenzyme Q junction, Q-junction; Complex II, CII; electron transfer system, ETS; fatty acid oxidation, FAO; flavin adenine dinucleotide, FAD/FADH<sub>2</sub>; nicotinamide adenine dinucleotide, NAD<sup>+</sup>/NADH; succinate dehydrogenase, SDH; tricarboxylic acid cycle, TCA
|keywords=[[coenzyme]]; [[cofactor]]; [[prosthetic group]]; coenzyme Q junction, Q-junction; Complex II, CII; [[H+-linked electron transfer |H<sup>+</sup>-linked electron transfer]]; [[electron transfer system]], ETS; [[matrix-ETS]]; [[membrane-ETS]]; fatty acid oxidation, FAO; flavin adenine dinucleotide, FAD/FADH<sub>2</sub>; nicotinamide adenine dinucleotide, NAD<sup>+</sup>/NADH; succinate dehydrogenase, SDH; tricarboxylic acid cycle, TCA; [[substrate]]; [[Gibbs force]]
|mipnetlab=AT Innsbruck Oroboros
|mipnetlab=AT Innsbruck Oroboros
}}
}}
ORC'''ID''': [[File:ORCID.png|20px|link=https://orcid.org/0000-0003-3647-5895]] Gnaiger Erich, Oroboros Instruments, Innsbruck, Austria
__TOC__
__TOC__
[[File:N-S FADH2-FMNH2.png|right|500px]]
::::'''» ''Links:''''' [[Ambiguity crisis]], [[Complex II ambiguities]], [[:Category:Ambiguity crisis - NAD and H+ |Complex I and hydrogen ion ambiguities in the electron transfer system]]
'''Figure 1. Complex II (SDH) bridges H+-linked electron transfer from the TCA cycle (matrix-ETS) to the electron transfer system (membrane-ETS) of the mt-inner membrane (mtIM).''' '''(a)''' NADH+H<sup>+</sup> and '''(b)''' succinate are substrates of 2{H<sup>+</sup>+e<sup>-</sup>} transfer to CI and CII, respectively, with prosthetic groups FMN and FAD as the corresponding electron acceptors. '''(c)''' Symbolic representation of ETS pathway architecture. Electron flow converges at the N-junction (NAD<sup>+</sup> → NADH+H<sup>+</sup>). Electron flow from NADH and succinate S converges through CI and CII at the Q-junction. CIII passes electrons to cytochrome ''c'' and in CIV to molecular O<sub>2</sub>, 2{H<sup>+</sup>+e<sup>-</sup>}+0.5 O<sub>2</sub> ⇢ H<sub>2</sub>O. '''(d)''' NADH+H<sup>+</sup> and NAD<sup>+</sup> cycle between matrix-dehydrogenases and CI, whereas FAD and FADH<sub>2</sub> cycle permanently bound within the same enzyme CII. Succinate and fumarate indicate the chemical entities irrespective of ionization, but charges are shown in NADH, NAD<sup>+</sup>, and H<sup>+</sup>. Joint pairs of half-circular arrows distinguish electron transfer 2{H<sup>+</sup>+e­<sup>-</sup>} to CI and CII from vectorial H<sup>+</sup> translocation across the mtIM (H<sup>+</sup><sub>neg</sub> → H<sup>+</sup><sub>pos</sub>). CI and CIII pump hydrogen ions from the negatively (neg) to the positively charged compartment (pos). '''(e)''' Iconic representation of SDH subunits. SDHA catalyzes the oxidation succinate → fumarate + 2{H<sup>+</sup>+e<sup>-</sup>} and reduction FAD + 2{H<sup>+</sup>+e<sup>-</sup>} → FADH<sub>2</sub> in the soluble domain of CII. The iron–sulfur protein SDHB transfers electrons through Fe-S clusters to the mtIM domain where ubiquinone UQ is reduced to ubiquinol UQH<sub>2</sub> in SDHC and SDHD.
:::: '''Acknowledgements''': I thank [[Cardoso Luiza HD |Luiza H.D. Cardoso]], [[Schmitt Sabine |Sabine Schmitt]], and [[Donnelly Chris |Chris Donnelly]] for stimulating discussions, and [[Cocco Paolo |Paolo Cocco]] for expert help on the graphical abstract and Figures 1d and e. The constructive comments of an anonymous reviewer (J Biol Chem) are explicitly acknowledged. Contribution to the European Union’s Horizon 2020 research and innovation program Grant 857394 ([[FAT4BRAIN]]).
 
[[File:FAO.png|right|600px]]
'''Figure 4. Fatty acid oxidation''' through the β-oxidation cycle (β-ox), the multi-enzyme electron transferring flavoprotein Complex (CETF, ETF:ETFDH; see text), and Complex I (CI) with convergent electron transfer into the Q-junction.
 
:::: '''Acknowledgements''': I thank Luiza H. Cardoso and Sabine Schmitt for stimulating discussions, and Paolo Cocco for expert help on the graphical abstract and Figures 1d and e. The constructive comments of an anonymous reviewer (J Biol Chem) are explicitly acknowledged. Contribution to the European Union’s Horizon 2020 research and innovation program Grant 857394 (FAT4BRAIN).
 
== Supplement 1. Footnotes on terminology ==
 
:::* [[Coenzyme]]:
::::: ‘The dissociable, low-relative-molecular-mass active group of an enzyme which transfers chemical groups, hydrogen, or electrons. A coenzyme binds with its associated protein (apoenzyme) to form the active enzyme (holoenzyme) (Burtis, Geary 1994). ‘A low-molecular-weight, non-protein organic compound participating in enzymatic reactions as dissociable acceptor or donor of chemical groups or electrons’ - https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:23354 (CHEBI:23354, retrieved 2023-06-21). A coenzyme or cosubstrate is a cofactor that is attached loosely and transiently to an enzyme. NADH is listed as a coenzyme, which should be regarded as a substrate of pyridine-linked dehydrogenases (Lehninger 1975).
 
:::* [[Cofactor]]:
::::: A cofactor is 'an organic molecule or ion (usually a metal ion) that is required by an enzyme for its activity. It may be attached either loosely (coenzyme) or tightly (prosthetic group)' - https://www.ebi.ac.uk/chebi/searchId.do?chebiId=23357 (CHEBI:23357, retrieved 2023-06-21).
 
:::* [[Electron transfer system]] ETS:
::::: The ''convergent'' architecture of the electron transfer ''system'' is emphasized in contrast to ''linear'' electron transfer ''chains'' ETCs within segments of the ETS.
 
:::* Electron transfer:
::::: A distinction is necessary between electron transfer in redox reactions and electron transport (translocation) in the diffusion of charged ionic species within or between cellular compartments. The symbol 2{H<sup>+</sup>+e<sup>−</sup>} is introduced to indicate H<sup>+</sup>-linked electron transfer of two hydrogen ions and two electrons in a redox reaction.
 
:::* Gibbs force:
::::: In contrast to the extensive quantity Gibbs energy [J], Gibbs force [J·mol<sup>-1</sup>] is an intensive quantity expressed as the partial derivative of Gibbs energy [J] per advancement of a reaction [mol] (Gnaiger 1993; 2020).
 
:::* H<sup>+</sup>-linked electron transfer:
::::: The term H<sup>+</sup>-coupled electron transfer ([[Hsu 2022 J Chem Phys |Hsu et al 2022]]) is replaced by H<sup><sup>+</sup></sup>-linked electron transfer, to avoid confusion with ''coupled'' H<sup>+</sup> translocation.
 
:::* Matrix-ETS:
::::: Electron transfer and corresponding OXPHOS capacities are classically studied in mitochondrial preparations as oxygen consumption supported by various fuel substrates undergoing partial oxidation in the mt-matrix, such as pyruvate, malate, succinate, and others. Therefore, the matrix component of ETS (matrix-ETS) is distinguished from the ETS bound to the mt-inner membrane (membrane-ETS; [[BEC_2020.1_doi10.26124bec2020-0001.v1 |Gnaiger et al 2020]]).
 
:::* Membrane-ETS:
::::: Electron transfer is frequently considered as the segment of redox reactions linked to the mtIM. However, the membrane-ETS is only part of the total ETS, which includes the upstream matrix-ETS.
 
:::* Misinformation:
::::: Misinformation is the mistaken sharing of the same content ([[Wardle 2023 Issues Sci Technol |Wardle 2023]]).
 
:::* [[Prosthetic group]]:
::::: A prosthetic group is a cofactor that is ‘a tightly bound, specific nonpolypeptide unit in a protein determining and involved in its biological activity’ - https://www.ebi.ac.uk/chebi/searchId.do?chebiId=CHEBI:26348 (CHEBI:26348, retrieved 2023-06-21). A prosthetic group is attached permanently and tightly or even covalently to an enzyme and that is regenerated in each enzymatic turnover. FAD is the prosthetic group of flavin-linked dehydrogenases, covalently bound to CII.
 
:::* [[Substrate]]:
::::: A substrate in a chemical reaction has a negative stoichiometric number since it is consumed, whereas a product has a positive stoichiometric number since it is produced. The general definition of a substrate in an enzyme-catalized reaction relies on the definition of the chemical reaction, without restriction to the nature of the substrate, i.e. independent of the substrate being a chemical entity in solution or a loosely bound cosubstrate (coenzyme) or even a tightly bound prosthetic group. The latter may be explicitly distinguished as a bound (internal) substrate from a free (external) substrate. Even different substrate pools may coexist (CoQ).
 
:::* 2{H<sup>+</sup>+e<sup>-</sup>}
::::: In H<sup>+</sup>-linked two-electron transfer, 2H<sup>+</sup> + 2e<sup>-</sup>, ‘the terms reducing equivalents or electron equivalents are used to refer to electrons and/or hydrogen atoms participating in oxidoreductions’ (Lehninger 1975). The symbol 2[H] is frequently used to distinguish reducing equivalents in the transfer from hydrogen donors to hydrogen acceptors from aqueous H<sup>+</sup>. Acid-base reactions obtain equilibrium fast without catalyst, whereas the slow oxidation-reduction reactions require an enzyme to proceed. However, 2[H] does not explicitly express that it applies to both electron and hydrogen ion transfer. Brackets are avoided to exclude the confusion with amount-of-substance concentrations frequently indicated by brackets. H<sup>+</sup>-linked two-electron transfer 2{H<sup>+</sup>+e<sup>-</sup>} is distinguished from single-electron transfer {H<sup>+</sup>}+{e<sup>-</sup>}.
 
 
== Beyond version 6 ==
''Last update: 2023-09-16''
 
::: <big>'''From CGpDH to FADH<sub>2</sub> to CII?'''</big>
 
[[File:Blanco 2017 Academic Press CORRECTION.png|300px|link=Blanco 2017 Academic Press]] <big><big>///</big></big> [[File:Willson 2022 Blood CORRECTION.png|300px|link=Willson 2022 Blood]]  <big><big>///</big></big>  [[File:Rai 2022 G3 (Bethesda) CORRECTION.png|300px|link=Rai 2022 G3 (Bethesda)]] <big><big>///</big></big> [[File:Koopman 2016 Nat Protoc CORRECTION.png|300px|link=Koopman 2016 Nat Protoc]]
:::: ''Comment'' ([[Cardoso Luiza]], [[Gnaiger Erich]], 2023-08-06):
'''Fig. 9.19 from [[Blanco 2017 Academic Press| Blanco, Blanco (2017)]]''', '''Fig. 1 from [[Willson 2022 Blood| Willson et al (2022)]]''', and '''Fig. 1 from [[Rai 2022 G3 (Bethesda)| Rai et al (2022)]]''' show FADH<sub>2</sub> <span style="color:red">(1)</span> to be formed in the mitochondrial matrix from <span style="color:red">GPDH</span>, GPD2, or <span style="color:red">GPO1</span> (all indicating [[CGpDH]]) and from the TCA cycle ('''Fig. 1 [[Rai 2022 G3 (Bethesda)| Rai et al (2022)]]'''), then <span style="color:red">(2)</span> feeding electrons further '<span style="color:red">To respiratory chain</span>', the 'ETC', or 'Electron Transport Chain' ([[ETS]]). Combined with FADH<sub>2</sub> shown <span style="color:red">(1)</span> to be formed in the mt-matrix from the TCA cycle and <span style="color:red">(2)</span> feeding into CII ('''Fig. 1 from [[Koopman 2016 Nat Protoc| Koopman et al (2016)]]'''; among >120 examples discussed as CII-[[Ambiguity crisis |ambiguities]]), one may arrive at the erroneous conclusion on a direct role of CII in the oxidation of glycerophosphate, analogous to false representations of CII involved in fatty acid oxidation.
 
<big>'''Addition to Figure 5: FAO and CII ambiguitiy'''</big>
 
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== Additions to 312 references on CII-ambiguities after publication of JBC 2024 ==
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Last update 2023-12-19
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<br>


:::: '''Add to Supplement 7'''


:::::: [[File:Stillway LW CORRECTION.png|300px]]
:::::: [[File:Thorgersen 2022 Front Microbiol CORRECTION.png|400px|link=Thorgersen 2022 Front Microbiol]]
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<br>


::: '''Beyond preprint'''


:::::: [[File:Grandoch 2019 Nat Metab CORRECTION.png|300px|link=Grandoch 2019 Nat Metab]]
:::::: [[File:Venkatachalam 2022 Cells CORRECTION.png|400px|link=Venkatachalam 2022 Cells]]
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:::::: '''NADH''' is shown as the '''''product''''' of the reaction catalyzed by CI in respiration. This error is rare in the literature, but comparable to the error frequenty encountered when '''FADH<sub>2</sub>''' is shown as the '''''substrate''''' of CII.
<br>


:::::: [[File:Lancaster 2002 Biochim Biophys Acta.png|300px|link=Lancaster 2002 Biochim Biophys Acta]] [[File:Lancaster 2001 FEBS Lett CORRECTION.png|300px|link=Lancaster 2001 FEBS Lett]]
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:::::: fumarate + 2H<sup>+</sup> shown besides NADH + H<sup>+</sup> is ambiguous.
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<br>


== Supplement 2. FAD a substrate of SDH and FADH<sub>2</sub> a substrate of CII ==
:::::: [[File:Wall 2006 Am J Physiol Heart Circ Physiol CORRECTION.png|400px|link=Wall 2006 Am J Physiol Heart Circ Physiol]]
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:::: '''Figure S2'''. Complex II ambiguities in graphical representations on FADH<sub>2</sub> as a substrate of Complex II in the canonical forward electron transfer. The TCA cycle reduces FAD to FADH<sub>2</sub> - in several cases shown to be catalyzed by SDH. Then FADH<sub>2</sub> is erroneously shown to feed electrons into CII. Alphabetical sequence of publications from 2001 to 2023.
<br>


:::::: [[File:Arnold, Finley 2022 CORRECTION.png|600px|link=Arnold 2023 J Biol Chem]]
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:::: Complex II ambiguities in graphical representations on FADH<sub>2</sub> as a substrate of Complex II in the canonical forward electron transfer. FADH → FAD+H ('''g'''), FADH<sub>2</sub> → FAD+2H<sup>+</sup> ('''a’''', '''c''', '''h-n'''), and FADH<sub>2</sub> → FAD ('''a''', '''b''', '''d-f''', '''o-θ''') should be corrected to FADH<sub>2</sub> → FAD (Eq. 3b). NADH → NAD<sup>+</sup> is frequently written in graphs without showing the H<sup>+</sup> on the left side of the arrow, except for ('''p-r'''). NADH → NAD<sup>+</sup>+H<sup>+</sup> ('''a-g''', '''m'''), NADH → NAD<sup>+</sup>+2H<sup>+</sup> ('''h-l'''), NADH+H<sup>+</sup> → NAD<sup>+</sup>+2H<sup>+</sup> ('''j''', '''k'''), and NADH → NAD ('''ι''') should be corrected to NADH+H<sup>+</sup> → NAD<sup>+</sup> (Eq. 3a). (Retrieved 2023-03-21 to 2023-05-04).
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<br>
 
 
== Supplement 3. FADH<sub>2</sub> a substrate of CII ==
 
:::: '''Figure S3'''. Complex II ambiguities in graphical representations on FADH<sub>2</sub> as a substrate of Complex II in the canonical forward electron transfer. Alphabetical sequence of publications from 2001 to 2023.
 
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:::: '''κ''' Risiglione P, Leggio L, Cubisino SAM, Reina S, Paternò G, Marchetti B, Magrì A, Iraci N, Messina A (2020) High-resolution respirometry reveals MPP+ mitochondrial toxicity mechanism in a cellular model of parkinson's disease. '''Int J Mol Sci''' 21:E7809. - [[Risiglione 2020 Int J Mol Sci |»Bioblast link«]]
<br>
 
:::::: [[File:Rodick 2018 Nutrition and Dietary Supplements CORRECTION.png|400px|link=Rodick 2018 Nutrition and Dietary Supplements]]
:::: '''λ''' Rodick TC, Seibels DR, Babu JR, Huggins KW, Ren G, Mathews ST (2018) Potential role of coenzyme Q10 in health and disease conditions. '''Nutrition and Dietary Supplements''' 10:1-11. - [[Rodick 2018 Nutrition and Dietary Supplements |»Bioblast link«]]
<br>
 
:::::: [[File:Sanchez et al 2001 CORRECTION.png|600px|link=Sanchez 2001 Br J Pharmacol]]
:::: '''μ''' Sanchez H, Zoll J, Bigard X, Veksler V, Mettauer B, Lampert E, Lonsdorfer J, Ventura-Clapier R (2001) Effect of cyclosporin A and its vehicle on cardiac and skeletal muscle mitochondria: relationship to efficacy of the respiratory chain. '''Br J Pharmacol''' 133:781-8. - [[Sanchez 2001 Br J Pharmacol |»Bioblast link«]]
<br>
 
:::::: [[File:Sarmah 2019 Transl Stroke Res CORRECTION.png|400px|link=Sarmah 2019 Transl Stroke Res]]
:::: '''ν''' Sarmah D, Kaur H, Saraf J, Vats K, Pravalika K, Wanve M, Kalia K, Borah A, Kumar A, Wang X, Yavagal DR, Dave KR, Bhattacharya P (2019) Mitochondrial dysfunction in stroke: implications of stem cell therapy. '''Transl Stroke Res''' doi: 10.1007/s12975-018-0642-y - [[Sarmah 2019 Transl Stroke Res |»Bioblast link«]]
 
:::::: [[File:Snyder 2009 Antioxid Redox Signal.png|400px|link=Snyder 2009 Antioxid Redox Signal]]
:::: '''ξ''' Snyder CM, Chandel NS (2009) Mitochondrial regulation of cell survival and death during low-oxygen conditions. '''Antioxid Redox Signal''' 11:2673-83. - [[Snyder 2009 Antioxid Redox Signal |»Bioblast link«]]
<br>
 
:::::: [[File:Srivastava 2016 Clin Transl Med CORRECTION.png|400px|link=Srivastava 2016 Clin Transl Med]]
:::: '''ο''' Srivastava S (2016) Emerging therapeutic roles for NAD(+) metabolism in mitochondrial and age-related disorders. '''Clin Transl Med''' 5:25. - [[Srivastava 2016 Clin Transl Med |»Bioblast link«]]
<br>
 
:::::: [[File:Szabo 2020 Int J Mol Sci CORRECTION.png|400px|link=Szabo 2020 Int J Mol Sci]]
:::: '''π''' Szabo L, Eckert A, Grimm A (2020) Insights into disease-associated tau impact on mitochondria. '''Int J Mol Sci''' 21:6344. - [[Szabo 2020 Int J Mol Sci |»Bioblast link«]]
<br>
 
:::::: [[File:Turton 2022 Int J Mol Sci CORRECTION.png|400px|link=Turton 2022 Int J Mol Sci]]
:::: '''σ''' Turton N, Cufflin N, Dewsbury M, Fitzpatrick O, Islam R, Watler LL, McPartland C, Whitelaw S, Connor C, Morris C, Fang J, Gartland O, Holt L, Hargreaves IP (2022) The biochemical assessment of mitochondrial respiratory chain disorders. '''Int J Mol Sci''' 23:7487. - [[Turton 2022 Int J Mol Sci |»Bioblast link«]]
<br>
 
:::::: [[File:Vekshin 2020 Springer Cham CORRECTION.png|400px|link=Vekshin 2020 Springer Cham]]
:::: '''τ''' Vekshin N (2020) Biophysics of mitochondria. '''Springer Cham''': 197 pp. - [[Vekshin 2020 Springer Cham |»Bioblast link«]]
<br>
 
:::::: [[File:Wang 2016 ACS Appl Mater Interfaces CORRECTION.png|400px|link=Wang 2016 ACS Appl Mater Interfaces]]
:::: '''υ''' Wang G, Feng H, Gao A, Hao Q, Jin W, Peng X, Li W, Wu G, Chu PK (2016) Extracellular electron transfer from aerobic bacteria to Au-loaded TiO2 semiconductor without light: a new bacteria-killing mechanism other than localized surface plasmon resonance or microbial fuel cells. '''ACS Appl Mater Interfaces''' 8:24509-16. - [[Wang 2016 ACS Appl Mater Interfaces |»Bioblast link«]]
<br>
 
:::::: [[File:Yepez 2018 PLOS One Fig1B.jpg|400px|link=Yepez 2018 PLOS One]]
:::: '''φ''' Yépez VA, Kremer LS, Iuso A, Gusic M, Kopajtich R, Koňaříková E, Nadel A, Wachutka L, Prokisch H, Gagneur J (2018) OCR-Stats: Robust estimation and statistical testing of mitochondrial respiration activities using Seahorse XF Analyzer. '''PLOS ONE''' 13:e0199938. - [[Yepez 2018 PLOS One |»Bioblast link«]]
<br>
 
:::::: [[File:Yuan 2022 Oxid Med Cell Longev CORRECTION.png|400px|link=Yuan 2022 Oxid Med Cell Longev]]
:::: '''χ''' Yuan Q, Zeng ZL, Yang S, Li A, Zu X, Liu J (2022) Mitochondrial stress in metabolic inflammation: modest benefits and full losses. '''Oxid Med Cell Longev''' 2022:8803404. - [[Yuan 2022 Oxid Med Cell Longev |»Bioblast link«]]
<br>
 
:::::: [[File:Zhang 2018 Mil Med Res CORRECTION.png|400px|link=Zhang 2018 Mil Med Res]]
:::: '''ψ''' Zhang H, Feng YW, Yao YM (2018) Potential therapy strategy: targeting mitochondrial dysfunction in sepsis. '''Mil Med Res''' 5:41. - [[Zhang 2018 Mil Med Res |»Bioblast link«]]
<br>
 
 
== Supplement 4. FADH<sub>2</sub> as substrate of CII and FAD + 2H<sup>+</sup> as products ==
 
:::: '''Figure S4'''. Complex II ambiguities: FADH<sub>2</sub> as substrate of CII and FAD + 2H<sup>+</sup> as products. Alphabetical sequence of publications from 2001 to 2023.
 
:::::: [[File:Ahmad 2022 StatPearls CORRECTION.png|400px|link=Ahmad 2022 StatPearls Publishing]]
:::: '''a''' Ahmad M, Wolberg A, Kahwaji CI (2022) Biochemistry, electron transport chain. '''StatPearls Publishing''' StatPearls [Internet]. Treasure Island (FL) - [[Ahmad 2022 StatPearls Publishing |»Bioblast link«]]
<br>
 
:::::: [[File:Chen 2022 Int J Mol Sci CORRECTION.png|400px|link=Chen 2022 Int J Mol Sci]]
:::: '''b''' Chen TH, Koh KY, Lin KM, Chou CK (2022) Mitochondrial dysfunction as an underlying cause of skeletal muscle disorders. '''Int J Mol Sci''' 23:12926. - [[Chen 2022 Int J Mol Sci |»Bioblast link«]]
<br>
 
:::::: [[File:El-Gammal 2022 Pflugers Arch CORRECTION.png|400px|link=El-Gammal 2022 Pflugers Arch]]
:::: '''c''' El-Gammal Z, Nasr MA, Elmehrath AO, Salah RA, Saad SM, El-Badri N (2022) Regulation of mitochondrial temperature in health and disease. '''Pflugers Arch''' 474:1043-51. - [[El-Gammal 2022 Pflugers Arch |»Bioblast link«]]
<br>
 
:::::: [[File:Hidalgo-Gutierrez CORRECTION.png|400px|link=Hidalgo-Gutierrez 2021 Antioxidants (Basel)]]
:::: '''d''' Hidalgo-Gutiérrez A, González-García P, Díaz-Casado ME, Barriocanal-Casado E, López-Herrador S, Quinzii CM, López LC (2021) Metabolic targets of coenzyme Q10 in mitochondria. '''Antioxidants (Basel)''' 10:520. - [[Hidalgo-Gutierrez 2021 Antioxidants (Basel) |»Bioblast link«]]
<br>
 
:::::: [[File:Payen 2019 Cancer Metastasis Rev CORRECTION.png|400px|link=Payen 2019 Cancer Metastasis Rev]]
:::: '''e''' Payen VL, Zampieri LX, Porporato PE, Sonveaux P (2019) Pro- and antitumor effects of mitochondrial reactive oxygen species. '''Cancer Metastasis Rev''' 38:189-203. - [[Payen 2019 Cancer Metastasis Rev |»Bioblast link«]]
<br>
 
:::::: [[File:Prasuhn 2021 Front Cell Dev Biol CORRECTION.png|400px|link=Prasuhn 2021 Front Cell Dev Biol]]
:::: '''f''' Prasuhn J, Davis RL, Kumar KR (2021) Targeting mitochondrial impairment in Parkinson's disease: challenges and opportunities. '''Front Cell Dev Biol''' 8:615461. - [[Prasuhn 2021 Front Cell Dev Biol |»Bioblast link«]]
<br>
 
:::::: [[File:Tseng 2022 Cells CORRECTION.png|400px|link=Tseng 2022 Cells]]
:::: '''g''' Tseng W-W, Wei A-C (2022) Kinetic mathematical modeling of oxidative phosphorylation in cardiomyocyte mitochondria. '''Cells''' 11:4020. - [[Tseng 2022 Cells |»Bioblast link«]]
<br>
 
:::::: [[File:Turton 2021 Expert Opinion Orphan Drugs CORRECTION.png|400px|link=Turton 2021 Expert Opinion Orphan Drugs]]
:::: '''h''' Turton N, Bowers N, Khajeh S, Hargreaves IP, Heaton RA (2021) Coenzyme Q10 and the exclusive club of diseases that show a limited response to treatment. '''Expert Opinion Orphan Drugs''' 9:151-60. - [[Turton 2021 Expert Opinion Orphan Drugs |»Bioblast link«]]
<br>
 
:::::: [[File:Yin 2021 FASEB J CORRECTION.png|400px|link=Yin 2021 FASEB J]]
:::: '''i''' Yin M, O'Neill LAJ (2021) The role of the electron transport chain in immunity. '''FASEB J''' 35:e21974. - [[Yin 2021 FASEB J |»Bioblast link«]]
 
 
== Supplement 5. FADH<sub>2</sub> as substrate of CII and FAD<sup>+</sup> as product ==
 
:::: '''Figure S5'''. Complex II ambiguities: FADH<sub>2</sub> as substrate of CII and FAD<sup>+</sup> as product. Alphabetical sequence of publications from 2001 to 2023.
 
:::::: [[File:Area-Gomez 2019 J Clin Invest CORRECTED.png|400px|link=Area-Gomez 2019 J Clin Invest]]
:::: '''a''' Area-Gomez E, Guardia-Laguarta C, Schon EA, Przedborski S (2019) Mitochondria, OxPhos, and neurodegeneration: cells are not just running out of gas. '''J Clin Invest''' 129:34-45. - [[Area-Gomez 2019 J Clin Invest |»Bioblast link«]]
<br>
 
:::::: [[File:Carriere 2019 Academic Press CORRECTION.png|400px|link=Carriere 2019 Academic Press]]
:::: '''b''' Carriere A, Casteilla L (2019) Role of mitochondria in adipose tissues metabolism and plasticity. Academic Press In: Mitochondria in obesity and type 2 diabetes. Morio B, Pénicaud L, Rigoulet M (eds) '''Academic Press'''. - [[Carriere 2019 Academic Press |»Bioblast link«]]
<br>
 
:::::: [[File:Fisher-Wellman 2012 Trends Endocrinol Metab Fig2 CORRECTION.png|700px|link=Fisher-Wellman 2012 Trends Endocrinol Metab]]
:::: '''c, d''' Fisher-Wellman KH, Neufer PD (2012) Linking mitochondrial bioenergetics to insulin resistance via redox biology. '''Trends Endocrinol Metab''' 23:142-53. - [[Fisher-Wellman 2012 Trends Endocrinol Metab |»Bioblast link«]]
<br>
 
:::::: [[File:Gero 2018 IntechOpen CORRECTION.png|400px|link=Gero 2018 IntechOpen]]
:::: '''e''' Gero D (2023) Hyperglycemia-induced endothelial dysfunction. '''IntechOpen''' Chapter 8. - [[Gero 2018 IntechOpen |»Bioblast link«]]
<br>
 
:::::: [[File:Onukwufor 2022 Antioxidants (Basel) CORRECTION.png|400px|link=Onukwufor 2022 Antioxidants (Basel)]]
:::: '''f''' Onukwufor JO, Dirksen RT, Wojtovich AP (2022) Iron dysregulation in mitochondrial dysfunction and Alzheimer's disease. '''Antioxidants (Basel)''' 11:692. - [[Onukwufor 2022 Antioxidants (Basel) |»Bioblast link«]]
<br>
 
:::::: [[File:Shirakawa 2023 Sci Rep CORRECTION.png|400px|link=Shirakawa 2023 Sci Rep]]
:::: '''g''' Shirakawa R, Nakajima T, Yoshimura A, Kawahara Y, Orito C, Yamane M, Handa H, Takada S, Furihata T, Fukushima A, Ishimori N, Nakagawa M, Yokota I, Sabe H, Hashino S, Kinugawa S, Yokota T (2023) Enhanced mitochondrial oxidative metabolism in peripheral blood mononuclear cells is associated with fatty liver in obese young adults. '''Sci Rep''' 13:5203. - [[Shirakawa 2023 Sci Rep |»Bioblast link«]]
:::::: While CI functions as a proton pump, CII does not. Depicting CII as a proton pump would be analogous to falsely portraying FADH<sub>2</sub> as the substrate of CII, as if it were a copy of CI, which functions as a proton pump with NADH as its substrate.
<br>
 
:::::: [[File:Sullivan 2014 Cell Cycle CORRECTION.png|400px|link=Sullivan 2014 Cell Cycle]]
:::: '''h''' Sullivan LB, Chandel NS (2014) Mitochondrial metabolism in TCA cycle mutant cancer cells. '''Cell Cycle''' 13:347-8. - [[Sullivan 2014 Cell Cycle |»Bioblast link«]]
<br>
 
:::::: [[File:Valle-Mendiola 2020 Cancers (Basel) CORRECTION.png|400px|link=Valle-Mendiola 2020 Cancers (Basel)]]
:::: '''i''' Valle-Mendiola A, Soto-Cruz I (2020) Energy metabolism in cancer: The roles of STAT3 and STAT5 in the regulation of metabolism-related genes. '''Cancers (Basel)''' 12:124. - [[Valle-Mendiola 2020 Cancers (Basel) |»Bioblast link«]]
<br>
 
== Supplement 6. FADH<sub>2</sub> or FADH as substrate of CII and FADH, FADH<sup>+</sup>, or FAD<sup>+</sup> as product ==
 
:::: '''Figure S6'''. Complex II ambiguities: FADH<sub>2</sub> as substrate of CII and FADH or FADH<sup>+</sup> as product. Sequence of publications from 2001 to 2023 according to (''4'') to (''9'').
 
:::::: [[File:Cadonic 2016 Mol Neurobiol CORRECTION.png|400px|link=Cadonic 2016 Mol Neurobiol]]
:::: '''a''' Cadonic C, Sabbir MG, Albensi BC (2016) Mechanisms of mitochondrial dysfunction in Alzheimer's disease. '''Mol Neurobiol''' 53:6078-90. - [[Cadonic 2016 Mol Neurobiol |»Bioblast link«]]
<br>
 
:::::: [[File:Kezic 2016 Oxid Med Cell Longev CORRECTION.png|400px|link=Kezic 2016 Oxid Med Cell Longev]]
:::: '''b''' Kezic A, Spasojevic I, Lezaic V, Bajcetic M (2016) Mitochondria-targeted antioxidants: future perspectives in kidney ischemia reperfusion injury. '''Oxid Med Cell Longev''' 2016:2950503. - [[Kezic 2016 Oxid Med Cell Longev |»Bioblast link«]]
<br>
 
:::::: [[File:Li 2013 J Hematol Oncol CORRECTION.png|400px|link=Li 2013 J Hematol Oncol]]
:::: '''c''' Li X, Fang P, Mai J, Choi ET, Wang H, Yang XF (2013) Targeting mitochondrial reactive oxygen species as novel therapy for inflammatory diseases and cancers. '''J Hematol Oncol''' 6:19. - [[Li 2013 J Hematol Oncol |»Bioblast link«]]
<br>
 
:::::: [[File:Tabassum 2020 J Biomed Res Environ Sci CORRECTION.png|400px|link=Tabassum 2020 J Biomed Res Environ Sci]]
:::: '''ρ''' Tabassum N, Kheya IS, Ibn Asaduzzaman SA, Maniha SM, Fayz AH, Zakaria A, Fayz AH, Zakaria A, Noor R (2020) A review on the possible leakage of electrons through the electron transport chain within mitochondria. '''J Biomed Res Environ Sci''' 1:105-13. - [[Tabassum 2020 J Biomed Res Environ Sci |»Bioblast link«]]
<br>
 
:::::: [[File:Yang 2020 Transl Neurodegener CORRECTION.png|400px|link=Yang 2020 Transl Neurodegener]]
:::: '''d''' Yang L, Youngblood H, Wu C, Zhang Q (2020) Mitochondria as a target for neuroprotection: role of methylene blue and photobiomodulation. '''Transl Neurodegener''' 9:19. - [[Yang 2020 Transl Neurodegener |»Bioblast link«]]
<br>
 
:::::: [[File:Torres 2017 Cell Metab CORRECTION.png|400px|link=Torres 2018 Cell Metab]]
:::: '''e''' Torres MJ, Kew KA, Ryan TE, Pennington ER, Lin CT, Buddo KA, Fix AM, Smith CA, Gilliam LA, Karvinen S, Lowe DA, Spangenburg EE, Zeczycki TN, Shaikh SR, Neufer PD (2018) 17β-estradiol directly lowers mitochondrial membrane microviscosity and improves bioenergetic function in skeletal muscle. '''Cell Metab''' 27:167-79. - [[Torres 2018 Cell Metab |»Bioblast link«]]
<br>
 
:::::: [[File:Johnson 2013 Eukaryot Cell CORRECTION.png|400px|link=Johnson 2013 Eukaryot Cell]]
:::: '''f''' Johnson X, Alric J (2013) Central carbon metabolism and electron transport in Chlamydomonas reinhardtii: metabolic constraints for carbon partitioning between oil and starch. '''Eukaryot Cell''' 12:776-93. - [[Johnson 2013 Eukaryot Cell |»Bioblast link«]]
<br>
 
 
:::::: [[File:Middleton 2021 Therap Adv CORRECTION.png|400px|link=Middleton 2021 Therap Adv Gastroenterol]]
:::: '''g''' Middleton P, Vergis N (2021) Mitochondrial dysfunction and liver disease: role, relevance, and potential for therapeutic modulation. '''Therap Adv Gastroenterol''' 14:17562848211031394. - [[Middleton 2021 Therap Adv Gastroenterol |»Bioblast link«]]
<br>
 
:::::: [[File:Puntel 2013 Toxicol In Vitro CORRECTION.png|400px|link=Puntel 2013 Toxicol In Vitro]]
:::: '''h''' Puntel RL, Roos DH, Seeger RL, Rocha JB (2013) Mitochondrial electron transfer chain complexes inhibition by different organochalcogens. '''Toxicol In Vitro''' 27:59-70. - [[Puntel 2013 Toxicol In Vitro |»Bioblast link«]]
<br>
 
:::::: [[File:Xing 2022 Atlantis Press CORRECTION.png|400px|link=Xing 2022 Atlantis Press]]
:::: '''i''' Xing Yunxie (2022) Is genome instability a significant cause of aging? A review. '''Atlantis Press'''. - [[Xing 2022 Atlantis Press |»Bioblast link«]]
<br>
 
 
== Supplement 7. FADH<sub>2</sub> or FADH as substrate of CII in websites ==
 
:::: '''Figure S7'''. Complex II ambiguities in graphical representations on FADH<sub>2</sub> as a substrate of Complex II in the canonical forward electron transfer. FADH → FAD+H ('''g'''), FADH<sub>2</sub> → FAD+2H<sup>+</sup> ('''a’''', '''c''', '''h-n'''), and FADH<sub>2</sub> → FAD ('''a''', '''b''', '''d-f''', '''o-θ''') should be corrected to FADH<sub>2</sub> → FAD (Eq. 3b). NADH → NAD<sup>+</sup> is frequently written in graphs without showing the H<sup>+</sup> on the left side of the arrow, except for ('''p-r'''). NADH → NAD<sup>+</sup>+H<sup>+</sup> ('''a-g''', '''m'''), NADH → NAD<sup>+</sup>+2H<sup>+</sup> ('''h-l'''), NADH+H<sup>+</sup> → NAD<sup>+</sup>+2H<sup>+</sup> ('''j''', '''k'''), and NADH → NAD ('''ι''') should be corrected to NADH+H<sup>+</sup> → NAD<sup>+</sup> (Eq. 3a). (Retrieved 2023-03-21 to 2023-05-04).


:::::: [[File:OpenStax Biology.png|400px]]
:::::: [[File:OpenStax Biology.png|400px]]
Line 957: Line 292:
:::: '''Website 48''' ('''ι'''): [https://chem.libretexts.org/Courses/Saint_Marys_College_Notre_Dame_IN/CHEM_118_(Under_Construction)/CHEM_118_Textbook/12%3A_Metabolism_(Biological_Energy)/12.4%3A_The_Citric_Acid_Cycle_and_Electron_Transport - LibreTexts Chemistry] - The Citric Acid Cycle and Electron Transport – Fig. 12.4.3
:::: '''Website 48''' ('''ι'''): [https://chem.libretexts.org/Courses/Saint_Marys_College_Notre_Dame_IN/CHEM_118_(Under_Construction)/CHEM_118_Textbook/12%3A_Metabolism_(Biological_Energy)/12.4%3A_The_Citric_Acid_Cycle_and_Electron_Transport - LibreTexts Chemistry] - The Citric Acid Cycle and Electron Transport – Fig. 12.4.3


:::::: [[File:Stillway LW CORRECTION.png|300px]]
:::: '''xx''' Stillway L William (2017) CHAPTER 9 Bioenergetics and Oxidative Metabolism. In: [https://doctorlib.info/medical/biochemistry/11.html Medical Biochemistry]
<br>


== Supplement 8. Weblinks on FAO and CII ==
 
<big>'''from FAO and CII ambiguitiy to CII as a H<sup>+</sup> in websites'''</big>
 
:::::: [[File:CHM333 LECTURES CORRECTION.png|250px]]
:::: '''xx''' [https://www.chem.purdue.edu/courses/chm333/Spring%202013/Lectures/Spring%202013%20Lecture%2037%20-%2038.pdf CHM333 LECTURES 37 & 38: 4/27 – 29/13 SPRING 2013 Professor Christine Hrycyna]
<br>


  (retrieved 2023-03-21 to 2023-05-02)
  (retrieved 2023-03-21 to 2023-05-02)
Line 967: Line 310:
:::: '''Website 51''': [https://www.chem.purdue.edu/courses/chm333/Spring%202013/Lectures/Spring%202013%20Lecture%2037%20-%2038.pdf CHM333 LECTURES 37 & 38: 4/27 – 29/13 SPRING 2013 Professor Christine Hrycyna]: Acyl-CoA dehydrogenase is listed under 'Electron transfer in Complex II'.
:::: '''Website 51''': [https://www.chem.purdue.edu/courses/chm333/Spring%202013/Lectures/Spring%202013%20Lecture%2037%20-%2038.pdf CHM333 LECTURES 37 & 38: 4/27 – 29/13 SPRING 2013 Professor Christine Hrycyna]: Acyl-CoA dehydrogenase is listed under 'Electron transfer in Complex II'.


== Supplement 9. CII as a proton pump ==
:::: '''Figure S9'''. Complex II as a proton pump
:::::: [[File:Cronshaw 2019 Photobiomodul Photomed Laser Surg CORRECTION.png|400px|link=Cronshaw 2019 Photobiomodul Photomed Laser Surg]]
:::: '''a''' Cronshaw M, Parker S, Arany P (2019) Feeling the heat: evolutionary and microbial basis for the analgesic mechanisms of photobiomodulation therapy. '''Photobiomodul Photomed Laser Surg''' 37:517-26. - [[Cronshaw 2019 Photobiomodul Photomed Laser Surg |»Bioblast link«]]
<br>
:::::: [[File:Jian 2020 Cell Metab CORRECTION.png|400px|link=Jian 2020 Cell Metab]]
:::: '''b''' Jian C, Fu J, Cheng X, Shen LJ, Ji YX, Wang X, Pan S, Tian H, Tian S, Liao R, Song K, Wang HP, Zhang X, Wang Y, Huang Z, She ZG, Zhang XJ, Zhu L, Li H (2020) Low-dose sorafenib acts as a mitochondrial uncoupler and ameliorates nonalcoholic steatohepatitis. '''Cell Metab''' 31:892-908. - [[Jian 2020 Cell Metab |»Bioblast link«]] 
:::::: While CI functions as a proton pump, CII does not. Depicting CII as a proton pump would be analogous to falsely portraying FADH<sub>2</sub> as the substrate of CII, as if it were a copy of CI, which functions as a proton pump with NADH as its substrate.
<br>
:::::: [[File:Shirakawa 2023 Sci Rep CORRECTION.png|400px|link=Shirakawa 2023 Sci Rep]]
:::: '''c''' Shirakawa R, Nakajima T, Yoshimura A, Kawahara Y, Orito C, Yamane M, Handa H, Takada S, Furihata T, Fukushima A, Ishimori N, Nakagawa M, Yokota I, Sabe H, Hashino S, Kinugawa S, Yokota T (2023) Enhanced mitochondrial oxidative metabolism in peripheral blood mononuclear cells is associated with fatty liver in obese young adults. '''Sci Rep''' 13:5203. - [[Shirakawa 2023 Sci Rep |»Bioblast link«]]
:::::: While CI functions as a proton pump, CII does not. Depicting CII as a proton pump would be analogous to falsely portraying FADH<sub>2</sub> as the substrate of CII, as if it were a copy of CI, which functions as a proton pump with NADH as its substrate.
<br>


:::::: [[File:Expii-Gabi Slizewska CORRECTION.png|400px]]
:::::: [[File:Expii-Gabi Slizewska CORRECTION.png|400px]]
:::: '''d''': [https://www.expii.com/t/electron-transport-chain-summary-diagrams-10139 expii expii - Image source: By Gabi Slizewska]: ‘FADH<sub>2</sub> from glycolysis and Krebs cycle is oxidized to FAD by Complex II. It also releases H<sup>+</sup> ions into the intermembrane space and passes off electrons’ (retrieved 2023-05-04).
:::: '''xx''': [https://www.expii.com/t/electron-transport-chain-summary-diagrams-10139 expii expii - Image source: By Gabi Slizewska]: ‘FADH<sub>2</sub> from glycolysis and Krebs cycle is oxidized to FAD by Complex II. It also releases H<sup>+</sup> ions into the intermembrane space and passes off electrons’ (retrieved 2023-05-04).


:::::: [[File:BioNinja 1 CORRECTION.png|400px]]
:::::: [[File:BioNinja 1 CORRECTION.png|400px]]
:::::: [[File:BioNinja 2 CORRECTION.png|400px]]
:::::: [[File:BioNinja 2 CORRECTION.png|400px]]
:::: '''e''','''f''': [https://ib.bioninja.com.au/higher-level/topic-8-metabolism-cell/untitled/electron-transport-chain.html BioNinja] (retrieved 2023-05-04).
:::: '''xx''': [https://ib.bioninja.com.au/higher-level/topic-8-metabolism-cell/untitled/electron-transport-chain.html BioNinja] (retrieved 2023-05-04).
 


{{Template:Keywords: Substrates and cofactors}}
{{Template:Keywords: Substrates and cofactors}}
== Cited by ==
{{Template:Cited by Gnaiger 2024 MitoFit}}
[[Category:Ambiguity crisis - CII and FADH2]]
{{Labeling
{{Labeling
|area=Patients, mt-Awareness
|enzymes=Complex II;succinate dehydrogenase
|enzymes=Complex II;succinate dehydrogenase
|additional=Ambiguity crisis, FAT4BRAIN, Publication:FAT4BRAIN
|additional=Ambiguity crisis, FAT4BRAIN, Publication:FAT4BRAIN
}}
}}

Latest revision as of 08:48, 1 May 2024

Publications in the MiPMap
Gnaiger E (2023) Complex II ambiguities ― FADH2 in the electron transfer system. MitoFit Preprints 2023.3.v6. https://doi.org/10.26124/mitofit:2023-0003.v6 - Published 2023-11-22 J Biol Chem (2024)

» MitoFit Preprints 2023.3.v6.

MitoFit pdf

Complex II ambiguities ― FADH2 in the electron transfer system

Gnaiger Erich (2023) MitoFit Prep

Abstract:

CII-ambiguities Graphical abstract.png
Gnaiger E (2024) Complex II ambiguities ― FADH2 in the electron transfer system. J Biol Chem 300:105470. https://doi.org/10.1016/j.jbc.2023.105470
Version 6 (v6) 2023-06-21
Version 5 (v5) 2023-05-31, (v4) 2023-05-12, (v3) 2023-05-04, (v2) 2023-04-04, (v1) 2023-03-24 - »Link to all versions«

The prevailing notion that reduced cofactors NADH and FADH2 transfer electrons from the tricarboxylic acid cycle to the mitochondrial electron transfer system creates ambiguities regarding respiratory Complex II (CII). The succinate dehydrogenase subunit SDHA of CII oxidizes succinate and reduces the covalently bound prosthetic group FAD to FADH2 in the canonical forward tricarboxylic acid cycle. However, several graphical representations of the electron transfer system depict FADH2 in the mitochondrial matrix as a substrate to be oxidized by CII. This leads to the false conclusion that FADH2 from the β-oxidation cycle in fatty acid oxidation feeds electrons into CII. In reality, dehydrogenases of fatty acid oxidation channel electrons to the coenzyme Q-junction but not through CII. The ambiguities surrounding Complex II in the literature and educational resources call for quality control, to secure scientific standards in current communications of bioenergetics, and ultimately support adequate clinical applications. This review aims to raise awareness of the inherent ambiguity crisis, complementing efforts to address the well-acknowledged issues of credibility and reproducibility.
• Keywords: coenzyme; cofactor; prosthetic group; coenzyme Q junction, Q-junction; Complex II, CII; H+-linked electron transfer; electron transfer system, ETS; matrix-ETS; membrane-ETS; fatty acid oxidation, FAO; flavin adenine dinucleotide, FAD/FADH2; nicotinamide adenine dinucleotide, NAD+/NADH; succinate dehydrogenase, SDH; tricarboxylic acid cycle, TCA; substrate; Gibbs force

• O2k-Network Lab: AT Innsbruck Oroboros

» Links: Ambiguity crisis, Complex II ambiguities, Complex I and hydrogen ion ambiguities in the electron transfer system
Acknowledgements: I thank Luiza H.D. Cardoso, Sabine Schmitt, and Chris Donnelly for stimulating discussions, and Paolo Cocco for expert help on the graphical abstract and Figures 1d and e. The constructive comments of an anonymous reviewer (J Biol Chem) are explicitly acknowledged. Contribution to the European Union’s Horizon 2020 research and innovation program Grant 857394 (FAT4BRAIN).

Additions to 312 references on CII-ambiguities after publication of JBC 2024

Last update 2023-12-19
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Supplement: FADH2 or FADH as substrate of CII in websites

Complex II ambiguities in graphical representations on FADH2 as a substrate of Complex II in the canonical forward electron transfer. FADH → FAD+H (g), FADH2 → FAD+2H+ (a’, c, h-n), and FADH2 → FAD (a, b, d-f, o-θ) should be corrected to FADH2 → FAD (Eq. 3b). NADH → NAD+ is frequently written in graphs without showing the H+ on the left side of the arrow, except for (p-r). NADH → NAD++H+ (a-g, m), NADH → NAD++2H+ (h-l), NADH+H+ → NAD++2H+ (j, k), and NADH → NAD (ι) should be corrected to NADH+H+ → NAD+ (Eq. 3a). (Retrieved 2023-03-21 to 2023-05-04).
OpenStax Biology.png
(a)
Website 1 (a,b): 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 (a,b): Concepts of Biology - 1st Canadian Edition by Charles Molnar and Jane Gair - Fig. 4.19a
Website 3 (a,b): Pharmaguideline
Website 4 (a,b): Texas Gateway - Figure 7.11
Website 5 (a,b): - CUNY
Website 6 (a,b): lumen Biology for Majors I - Fig. 1
Website 7 (a): LibreTexts Biology Oxidative Phosphorylation - Electron Transport Chain - Figure 7.11.1
Website 8 (a): - Brain Brooder
Khan Academy modified from OpenStax CORRECTION.png
(a’)
Website 9 (a’,b,v): 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 10 (a’,b,v): Saylor Academy
Expii OpenStax CORRECTION.png
(b)
Website 1 (a,b): OpenStax Biology - Fig. 7.12
Website 2 (a,b): Concepts of Biology - 1st Canadian Edition by Charles Molnar and Jane Gair - Fig. 4.19c
Website 3 (a,b): Pharmaguideline
Website 4 (a,b): Texas Gateway - Figure 7.13
Website 5 (a,b): - CUNY
Website 6 (a,b): lumen Biology for Majors I - Fig. 3
Website 9 (a’,b,v): Khan Academy - Image modified from "Oxidative phosphorylation: Figure 3," by Openstax College, Biology (CC BY 3.0)
Website 10 (a’,b,v): Saylor Academy
Website 11 (b,c,n,w,β): expii - Image source: By CNX OpenStax
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(c)
Website 11 (b,c,n,w,β): expii - Image source: By CNX OpenStax
Website 12 (c,t): ThoughtCo - extender01 / iStock / Getty Images Plus
Website 13 (c): wikimedia 30148497 - Anatomy & Physiology, Connexions Web site. http://cnx.org/content/col11496/1.6/, 2013-06-19
Website 14 (c): biologydictionary.net 2018-08-21
Website 15 (c): Quora
Website 16 (c): TeachMePhysiology - Fig. 1. 2023-03-13
Website 17 (c): toppr
Labxchange CORRECTION.png
(d)
Website 18 (d): Labxchange - Figure 8.15 credit: modification of work by Klaus Hoffmeier
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(e)
Website 19 (e): Jack Westin MCAT Courses
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(f)
Website 20 (f): videodelivery
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Website 21 (g): - SparkNotes
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Website 22 (h,t): researchtweet
Website 23 (h): Microbe Notes
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Website 24 (i): FlexBooks - CK-12 Biology for High School- 2.28 Electron Transport, Figure 2
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(j)
Website 25 (j): Labster Theory
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(k)
Website 26 (k): nau.edu
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(l)
Website 27 (l): ScienceFacts
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(m)
Website 28 (m): cK-12
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(n)
Website 11 (b,c,n,w,β): expii - Image source: By CNX OpenStax
Website 29 (n): Wikimedia
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Website 30 (o): creative-biolabs
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Website 31 (p): dreamstime
Website 32 (p): VectorMine
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(q)
Website 33: YouTube Dirty Medicine Biochemistry - Uploaded 2019-07-18
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(r)
Website 34 (r): DBriers
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Website 35 (s): SNC1D - BIOLOGY LESSON PLAN BLOG
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Website 12 (c,t): ThoughtCo - extender01 / iStock / Getty Images Plus
Website 22 (h,t): researchtweet
Website 36 (t): dreamstime
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Website 37 (u): hyperphysics
Khan Academy CORRECTION.png
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Website 9 (a’,b,v): Khan Academy
Website 10 (a’,b,v): Saylor Academy
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(w)
Website 11 (b,c,n,w,β): expii - Whitney, Rolfes 2002
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Website 38 (x): UrbanPro
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Website 39 (y): Quizlet
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Website 40 (z): unm.edu
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Website 41 (α): YouTube sciencemusicvideos - Uploaded 2014-08-19
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(β)
Website 11 (b,c,n,w,β): expii expii - Image source: By Gabi Slizewska
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Website 42 (γ): BiochemDen.com
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(δ)
Website 43 (δ): hopes, Huntington’s outreach project for education, at Stanford
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(ε)
Website 44 (ε): [ https://www.studocu.com/en-gb/document/university-college-london/mammalian-physiology/electron-transport-chain/38063777 studocu, University College London]
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(ζ)
Website 45 (ζ): ScienceDirect
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(η)
Website 46 (η): BBC BITESIZE cK-12
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(θ)
Website 47 (θ): freepik
LibreTexts Chemistry CORRECTION.png
(ι)
Website 48 (ι): - LibreTexts Chemistry - The Citric Acid Cycle and Electron Transport – Fig. 12.4.3
Stillway LW CORRECTION.png
xx Stillway L William (2017) CHAPTER 9 Bioenergetics and Oxidative Metabolism. In: Medical Biochemistry



from FAO and CII ambiguitiy to CII as a H+ in websites

CHM333 LECTURES CORRECTION.png
xx CHM333 LECTURES 37 & 38: 4/27 – 29/13 SPRING 2013 Professor Christine Hrycyna


(retrieved 2023-03-21 to 2023-05-02)
Website 49: Conduct Science: "In Complex II, the enzyme succinate dehydrogenase in the inner mitochondrial membrane reduce FADH2 to FAD+. Simultaneously, succinate, an intermediate in the Krebs cycle, is oxidized to fumarate." - Comments: FAD does not have a postive charge. FADH2 is the reduced form, it is not reduced. And again: In CII, FAD is reduced to FADH2.
Website 50: The Medical Biochemistry Page: ‘In addition to transferring electrons from the FADH2 generated by SDH, complex II also accepts electrons from the FADH2 generated during fatty acid oxidation via the fatty acyl-CoA dehydrogenases and from mitochondrial glycerol-3-phosphate dehydrogenase (GPD2) of the glycerol phosphate shuttle’ (Figure 8d).
Website 51: CHM333 LECTURES 37 & 38: 4/27 – 29/13 SPRING 2013 Professor Christine Hrycyna: Acyl-CoA dehydrogenase is listed under 'Electron transfer in Complex II'.


Expii-Gabi Slizewska CORRECTION.png
xx: expii expii - Image source: By Gabi Slizewska: ‘FADH2 from glycolysis and Krebs cycle is oxidized to FAD by Complex II. It also releases H+ ions into the intermembrane space and passes off electrons’ (retrieved 2023-05-04).
BioNinja 1 CORRECTION.png
BioNinja 2 CORRECTION.png
xx: BioNinja (retrieved 2023-05-04).


Questions.jpg


Click to expand or collaps
Bioblast links: Substrates and cofactors - >>>>>>> - Click on [Expand] or [Collapse] - >>>>>>>
Substrate
» Substrate
» Product
» Substrates as electron donors
» Cellular substrates
» MitoPedia: Substrates and metabolites
» Substrate-uncoupler-inhibitor titration
Cofactor
» Cofactor
» Coenzyme, cosubstrate
» Nicotinamide adenine dinucleotide
» Coenzyme Q2
» Prosthetic group
» Flavin adenine dinucleotide
Referennces
» Gnaiger E (2023) Complex II ambiguities ― FADH2 in the electron transfer system. MitoFit Preprints 2023.3.v6. https://doi.org/10.26124/mitofit:2023-0003.v6


Cited by

Gnaiger 2024 Ambiguity crisis.jpg
Gnaiger E (2024) Addressing the ambiguity crisis in bioenergetics and thermodynamics. MitoFit Preprints 2024.3. https://doi.org/10.26124/mitofit:2024-0003


Labels: MiParea: Patients, mt-Awareness 



Enzyme: Complex II;succinate dehydrogenase 



Ambiguity crisis, FAT4BRAIN, Publication:FAT4BRAIN 

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