Aggregation of Phosphates Enhances Enzyme Activity in Aqueous Solution.Chemphyschem 2026 May 14; 27(9):e202500806.C
Diffusion coefficients and viscosities of tetrabutylammonium dihydrogen phosphate ([NBu4][+][H2PO4][-]), potassium dihydrogen phosphate (K[+][H2PO4][-]), tetrabutylammonium bromide ([NBu4][+][Br][-]), tetrabutylammonium chloride ([NBu4][+][Cl][-]), and biologically relevant phosphate salts adenosine monophosphate (AMP), adenosine diphosphate (ADP), and adenosine triphosphate (ATP) were measured in aqueous solutions as a function of concentration across millimolar concentrations. The [NBu4][+] cation makes the solutions viscous at high millimolar concentrations, and there was no significant evidence of aggregation of the [H2PO4][-] anion. At higher millimolar concentrations, ATP, ADP, and AMP aggregate in aqueous solutions. The increasing concentration of ATP and ADP leads to increased activity of three different enzymes: cytochrome c, laccase, and horseradish peroxidase.
