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11:57
Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase
0 Views •
2025
Here, we describe a yeast system reconstituting human γ-secretase. This system allows for the identification and study of mutations affecting activity and for screening of γ-secretase inhibitors (GSIs). Utilizing the loss of function properties of familial Alzheimer's disease mutants, it is possible to screen for γ-secretase modulators (GSMs).
02:36
The Citric Acid Cycle
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2019
The citric acid cycle, also known as the Krebs cycle or TCA cycle, consists of several energy-generating reactions that yield one ATP molecule, three NADH molecules, one FADH2 molecule, and two CO2 molecules. Acetyl CoA is the point-of-entry into the citric acid cycle, which occurs in the inner membrane (i.e., matrix) of mitochondria in eukaryotic cells or the cytoplasm of prokaryotic cells. Prior to the citric acid cycle, pyruvate oxidation produced two acetyl CoA molecules per glucose...
01:28
Electron Transport Chains
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2019
The final stage of cellular respiration is oxidative phosphorylation that consists of two steps: the electron transport chain and chemiosmosis. The electron transport chain is a set of proteins found in the inner mitochondrial membrane in eukaryotic cells. Its primary function is to establish a proton gradient that can be used during chemiosmosis to produce ATP and generate electron carriers, such as NAD+ and FAD, that are used in glycolysis and the citric acid cycle. The ETC is comprised of...
07:47
Longitudinal In Vivo Imaging of the Cerebrovasculature: Relevance to CNS Diseases
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Cited by 9 •
2016
This manuscript describes a procedure to track the remodeling of the cerebrovasculature during amyloid plaque accumulation in vivo using longitudinal two-photon microscopy. A thinned-skull preparation enables the visualization of fluorescent dyes to assess the progression of cerebrovascular damage in a mouse model of Alzheimer's disease.
12:08
Monitoring the Reductive and Oxidative Half-Reactions of a Flavin-Dependent Monooxygenase using Stopped-Flow Spectrophotometry
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Cited by 12 •
2012
We describe the use of a stopped-flow instrument to investigate both the reductive and oxidative half-reactions of Aspergillus fumigatus siderophore A (SidA), a flavin-dependent monooxygenase. We then show the spectra corresponding to the species in the reaction of SidA and we calculate the rate constants for their formation.
FAQs
FAD accepts two hydrogen atoms during an enzyme-catalyzed reaction, producing FADH2. It can then release the transferred electrons and return to its oxidized form. This reversible cycling allows the same coenzyme system to support repeated redox reactions, linking individual enzyme activities with broader metabolic processes that depend on controlled electron movement.
FAD-dependent enzymes provide a molecular pathway for transferring electrons within specific metabolic reactions. Their activity connects the chemical breakdown of nutrients with downstream energy-related processes and also supports biosynthesis. Because these enzymes use FAD as part of their reaction machinery, changes in their function can affect several interconnected aspects of cellular metabolism.
The FAD to FADH2 transition temporarily captures reducing power as electrons and hydrogen atoms move through metabolism. FADH2 can later release electrons, allowing that stored reducing capacity to contribute to oxidative phosphorylation through the respiratory electron transport chain. This connection helps explain how metabolic reactions support the generation of usable cellular energy.
FAD supports electron-transfer reactions in both the citric acid cycle and fatty acid oxidation, so its role extends across different routes for processing nutrients. The reduced coenzyme generated in these reactions can also contribute to respiratory electron transport. This coordination links nutrient breakdown with energy conversion rather than limiting FAD to one pathway.
Riboflavin provides the source from which cells derive FAD, connecting vitamin-derived molecules with enzyme function and metabolism. Once available as FAD, the coenzyme can participate in reversible electron transfer. This relationship gives riboflavin biological significance beyond its origin, because the resulting coenzyme supports reactions involved in energy production and biosynthesis.
Studying FAD is useful when a metabolic disorder may involve impaired electron transfer or disrupted activity of FAD-dependent enzymes. Since these enzymes participate in energy production and biosynthesis, altered function can influence multiple cellular processes. Examining FAD-related reactions therefore helps connect molecular changes in metabolism with broader cellular consequences.
Research on FAD-dependent reactions can clarify how cells convert nutrients into usable chemical energy and how electron transfer is coordinated across metabolic pathways. It can also reveal how biosynthetic activity and energy production are interconnected. These outcomes make FAD a useful subject for interpreting normal metabolism as well as possible metabolic dysfunction.