Succinate dehydrogenase reduces FAD rather than NAD+ due to the thermodynamic reduction potential of the reaction

the verdict

SUPPORTED

the evidence backs this

Recorded sources

3 sources for · 0 against

Counts group repeated records of the same source within each side. They do not measure evidence strength or source independence.

Succinate dehydrogenase reduces enzyme-bound FAD rather than free NAD+ because of the specific thermodynamic reduction potentials governing the oxidation of succinate in cellular bioenergetics.

The analysis

The retrieved papers consistently confirm that succinate dehydrogenase (Complex II) interacts with FAD as its prosthetic group, and bioenergetic literature emphasizes that thermodynamic properties and redox potentials determine why specific electron carriers like FAD versus NAD+ are utilized in these metabolic reactions.

Evidence for · 3

Complex II ambiguities-FADH2 in the electron transfer system.

Recorded source metadata

Gnaiger E. Complex II ambiguities-FADH2 in the electron transfer system.. 2024. https://doi.org/10.1016/j.jbc.2023.105470

The paper explains that succinate dehydrogenase oxidizes succinate and reduces the covalently bound prosthetic group FAD within Complex II.

Source citation format

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More for · 2

Controlled power: how biology manages succinate-driven energy release.

Recorded source metadata

Mookerjee SA, Gerencser AA, Watson MA, Brand MD. Controlled power: how biology manages succinate-driven energy release.. 2021. https://doi.org/10.1042/bst20211032

This review highlights how the thermodynamic redox potentials and properties of succinate-driven reactions dictate mitochondrial energy release and distinct bioenergetic pathways compared to NAD-linked substrates.

Source citation format

Reduced Nucleotides, Thiols and O2 in Cellular Redox Balance: A Biochemist's View.

Recorded source metadata

Bettendorff L. Reduced Nucleotides, Thiols and O2 in Cellular Redox Balance: A Biochemist's View.. 2022. https://doi.org/10.3390/antiox11101877

The review notes that molecules such as NAD+ and FAD serve as specific electron acceptors during catabolic metabolism based on their physicochemical properties and redox roles.

Source citation format

The paper trail · every fact has a biography

first checked01 Aug 2026

judged → SUPPORTED · 8401 Aug 2026

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