NADH induces iron release from pea seed ferritin: a model for interaction between coenzyme and protein components in foodstuffs.

Plant ferritin from legume seeds co-exists with coenzyme NADH (a reduced form of nicotinamide-adenine dinucleotide) in many foodstuffs. In the present study, the interaction of NADH with apo pea seed ferritin (PSF) was investigated by fluorescence resonance energy transfer (FRET), fluorescence titration, transmission electron microscope (TEM), and isothermal titration calorimetry (ITC). We found that NADH molecules bound on the outer surface of PSF close to the 4-fold channels, which was 1.58 nm from tryptophan residue (Trp). Consequently, such binding facilitates iron release from holo PSF, which might have a negative effect on PSF as an iron supplement, while NADH was oxidised into NAD(+). However, the binding of NADH to the protein does not affect the entry of toxic ferrous ions into the apo protein shell, where these ferrous ions were oxidised into less toxic ferric ions. Moreover, NADH binding markedly affects the tertiary structure around Trp residues of PSF. These findings advanced our understanding of the interactions between different naturally occurring components in a complex food system.