Redox transfer
NAD+/NADH couples oxidation and reduction reactions across glycolysis, the citric-acid cycle and oxidative phosphorylation.


Research profile
Cellular redox cofactor research material
Nicotinamide adenine dinucleotide (NAD+) is a central redox cofactor used throughout cellular metabolism. It cycles between oxidised NAD+ and reduced NADH forms to transfer electrons and also serves as a substrate for enzymes including sirtuins and PARPs.
Scientific context
NAD+ research examines energy metabolism, mitochondrial function, redox balance, DNA-repair signalling and NAD-consuming enzyme activity. Direct NAD+ and NAD-precursor experiments are not interchangeable; transport, metabolism and compartmentalisation can produce different results.
Mechanism map
NAD+/NADH couples oxidation and reduction reactions across glycolysis, the citric-acid cycle and oxidative phosphorylation.
NAD+ is consumed by signalling and repair enzymes including sirtuins, PARPs and CD38-linked pathways.
Cytosolic, nuclear and mitochondrial NAD pools are regulated differently, making sampling location and timing critical.
Study design
These are experimental design concepts—not recommendations for human use, co-administration or dosing.
Supports factorial metabolic studies connecting receptor-level signalling with cellular redox and energy endpoints.
Use separate and combined arms; this is a study-design concept, not a human-use recommendation.Adds a defined matrix-remodelling axis to oxidative-stress or cellular-repair models.
Copper-dependent redox chemistry may alter assays, so include interference controls.May be used in preclinical designs connecting cellular energetics with repair-pathway readouts.
Evidence bases differ substantially; maintain single-agent controls.Interpretation controls
Evidence trail