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.v3. https://doi.org/10.26124/mitofit:2023-0003.v3
|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.v3. [[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 3 (v3) 2023-05-04''' [https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf 10.26124/mitofit:2023-0003.v3]
::: 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 2 (v2) 2023-04-04 [https://wiki.oroboros.at/images/a/ae/Gnaiger_2023_MitoFit_CII.pdf 10.26124/mitofit:2023-0003.v2]</small>
::: <small>Version 6 (v6) 2023-06-21 </small>
::: <small>Version 1 (v1) 2023-03-247 [https://wiki.oroboros.at/images/archive/a/ae/20230404153753%21Gnaiger_2023_MitoFit_CII.pdf 10.26124/mitofit:2023-0003] - [https://wiki.oroboros.at/index.php/File:Gnaiger_2023_MitoFit_CII.pdf »Link to all versions«]</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>
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 and the β-oxidation cycle in fatty acid oxidation. 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 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; Complex CII; electron transfer system; fatty acid oxidation; flavin adenine dinucleotide;succinate dehydrogenase; tricarboxylic acid cycle
|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
}}
}}
[[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>+e­<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 → fumarate+2{H<sup>+</sup>+e<sup>-</sup>} and reduction FAD+2{H<sup>+</sup>+e<sup>-</sup>} → FADH<sub>2</sub>. The iron–sulfur 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> ⇢ 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>.
ORC'''ID''': [[File:ORCID.png|20px|link=https://orcid.org/0000-0003-3647-5895]] 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 Union’s Horizon 2020 research and innovation program Grant 857394 (FAT4BRAIN).
__TOC__
__TOC__
Last update 2023-05-06
::::'''» ''Links:''''' [[Ambiguity crisis]], [[Complex II ambiguities]], [[:Category:Ambiguity crisis - NAD and H+ |Complex I and hydrogen ion ambiguities in the electron transfer system]]
== Supplement 1. Footnotes on terminology ==
:::: '''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]]).


::::* Electron transfer system ETS
== Additions to 312 references on CII-ambiguities after publication of JBC 2024 ==
::::: The convergent architecture of the electron transfer system is emphasized in contrast to linear electron transfer chains ETCs within segments of the ETS.
Last update 2023-12-19
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::::* 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.


::::* H+-linked electron transfer
:::::: [[File:Ben-Shachar 2009 J Neural Transm (Vienna) CORRECTION.png|400px|link=Ben-Shachar 2009 J Neural Transm (Vienna)]]
::::: 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.
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::::* 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
:::::: [[File:Bon 2022 J Clin Case Rep Stud CORRECTION.png|400px|link=Bon 2022 J Clin Case Rep Stud]]
::::: 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.
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::::* 2{H<sup>+</sup>+e<sup>-</sup>}: The symbol [2 H] is frequently used to indicate redox equivalents in the transfer from hydrogen donors to hydrogen acceptors. 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 their frequent application to indicate amount-of-substance concentrations.


== Supplement 2. FAD a substrate of SDH and FADH<sub>2</sub> a substrate of CII ==
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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>


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== 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.
:::::: [[File:Su 2020 Mol Biol Rep CORRECTION.png|400px|link=Su 2020 Mol Biol Rep]]
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<br>


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:::: '''Website 33''': [https://www.google.com/imgres?imgurl=https%3A%2F%2Fi.ytimg.com%2Fvi%2FLsRQ5_EmxJA%2Fmaxresdefault.jpg&tbnid=6w-0DVPMw7vOdM&vet=12ahUKEwjw2YO5--T9AhUwpCcCHduuDVgQMygDegUIARDzAQ..i&imgrefurl=https%3A%2F%2Fwww.youtube.com%2Fwatch%3Fv%3DLsRQ5_EmxJA&docid=bZxQYNch1Ys-VM&w=1280&h=720&q=electron%20transport%20chain&hl=en-US&client=firefox-b-d&ved=2ahUKEwjw2YO5--T9AhUwpCcCHduuDVgQMygDegUIARDzAQ YouTube Dirty Medicine Biochemistry] - Uploaded 2019-07-18


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::: ('''β''')
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== Supplement 4. FADH<sub>2</sub> as substrate of CII and FAD + 2H<sup>+</sup> as products ==
:::::: [[File:Freepik CORRECTION.png|400px]]
::: ('''θ''')
:::: '''Website 47''' ('''θ'''): [https://www.freepik.com/premium-vector/oxidative-phosphorylation-process-electron-transport-chain-final-step-cellular-respiration_29211885.htm freepik]


:::: '''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:LibreTexts Chemistry_CORRECTION.png|400px]]
 
::: ('''ι''')
####
:::: '''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


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:::::: [[File:Stillway LW CORRECTION.png|300px]]
:::: '''1''' 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«]]
:::: '''xx''' Stillway L William (2017) CHAPTER 9 Bioenergetics and Oxidative Metabolism. In: [https://doctorlib.info/medical/biochemistry/11.html Medical Biochemistry]
:::::: 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>
<br>


:::::: [[File:Tseng 2022 Cells CORRECTION.png|400px|link=Tseng 2022 Cells]]
:::: '''4''' 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:El-Gammal 2022 Pflugers Arch CORRECTION.png|400px|link=El-Gammal 2022 Pflugers Arch]]
<big>'''from FAO and CII ambiguitiy to CII as a H<sup>+</sup> in websites'''</big>
:::: '''6''' 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«]]
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:::: '''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>
<br>


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(retrieved 2023-03-21 to 2023-05-02)
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:::: '''Website 49''': [https://conductscience.com/electron-transport-chain/ Conduct Science]: "In Complex II, the enzyme succinate dehydrogenase in the inner mitochondrial membrane reduce FADH<sub>2</sub> to FAD<sup>+</sup>. Simultaneously, succinate, an intermediate in the Krebs cycle, is oxidized to fumarate." - Comments: FAD does not have a postive charge. FADH<sub>2</sub> is the reduced form, it is not reduced. And again: In CII, FAD is reduced to FADH<sub>2</sub>.
<br>


:::::: [[File:Xing 2022 Atlantis Press CORRECTION.png|400px|link=Xing 2022 Atlantis Press]]
:::: '''Website 50''': [https://themedicalbiochemistrypage.org/oxidative-phosphorylation-related-mitochondrial-functions/ The Medical Biochemistry Page]: ‘In addition to transferring electrons from the FADH<sub>2</sub> generated by SDH, complex II also accepts electrons from the FADH<sub>2</sub> 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).
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:::: '''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).
<br>
 
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:::::: 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>
 
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:::: '''27''' 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«]]
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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>
 
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<br>
 
=== Supplement Figure S1 (v2) ===
 
:::: '''Figure S1.''' Complex II ambiguities in graphical representations on FADH<sub>2</sub> as a substrate of Complex II in the canonical forward electron transfer. Chronological sequence of publications from 2001 to 2023.
<br>
 
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<br>
 
=== Supplement Figure S2 (v2) ===
 
:::: '''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 (retrieved 2023-03-21 to 2023-04-04)
 
:::::: [[File:OpenStax Biology.png|400px]]
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:::: '''Website 38''': [https://opentextbc.ca/biology/chapter/4-3-citric-acid-cycle-and-oxidative-phosphorylation/ Concepts of Biology] - Charles Molnar and Jane Gair. 4.3 Citric Acid Cycle and Oxidative Phosphorylation. Concepts of Biology - 1st Canadian Edition, BCcampus
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:::::: [[File:Khan Academy modified from OpenStax CORRECTION.png|400px]]
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:::::: [[File:Jack Westin CORRECTION.png|400px]]
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:::::: [[File:Labxchange CORRECTION.png|400px]]
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:::::: [[File:Biologydictionary.net CORRECTION.png|400px]]
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:::::: [[File:Creative-biolabs CORRECTION.png|400px]]
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:::::: [[File:Khan Academy CORRECTION.png|400px]]
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:::::: [[File:Expii-Whitney, Rolfes 2002 CORRECTION.png|400px]]
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{{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=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
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(d)
Website 18 (d): Labxchange - Figure 8.15 credit: modification of work by Klaus Hoffmeier
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Website 19 (e): Jack Westin MCAT Courses
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Website 20 (f): videodelivery
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Website 21 (g): - SparkNotes
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Website 22 (h,t): researchtweet
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Website 24 (i): FlexBooks - CK-12 Biology for High School- 2.28 Electron Transport, Figure 2
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Website 25 (j): Labster Theory
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Website 26 (k): nau.edu
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Website 27 (l): ScienceFacts
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Website 28 (m): cK-12
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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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Website 33: YouTube Dirty Medicine Biochemistry - Uploaded 2019-07-18
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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
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Website 9 (a’,b,v): Khan Academy
Website 10 (a’,b,v): Saylor Academy
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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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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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Website 43 (δ): hopes, Huntington’s outreach project for education, at Stanford
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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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Website 45 (ζ): ScienceDirect
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Website 46 (η): BBC BITESIZE cK-12
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Website 47 (θ): freepik
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Website 48 (ι): - LibreTexts Chemistry - The Citric Acid Cycle and Electron Transport – Fig. 12.4.3
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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

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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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