Succinate dehydrogenase reduces FAD rather than NAD+ due to the thermodynamic reduction potential of the reaction
the verdict
SUPPORTED
the evidence backs this
confidence 84/100
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.
Evidence for · 3
Complex II ambiguities-FADH<sub>2</sub> in the electron transfer system.
2024 · cited by 30
The paper explains that succinate dehydrogenase oxidizes succinate and reduces the covalently bound prosthetic group FAD within Complex II.
See more details
More for · 2
Controlled power: how biology manages succinate-driven energy release.
2021 · cited by 10
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.
Reduced Nucleotides, Thiols and O<sub>2</sub> in Cellular Redox Balance: A Biochemist's View.
2022 · cited by 4
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.