Nuclear magnetic resonance (NMR) spectroscopy has proven a unique approach to investigate the kinetics of chemical and enzyme reactions, by allowing simultaneous identification and monitoring of both their substrates and products. However, the low sensitivity of NMR often limits its application to reactions with slow time scales. This can be overcome using dissolution dynamic nuclear polarization (dDNP) techniques. Thus, by hyperpolarizing magnetically active nuclei at cryogenic temperatures, and by observing their signals in ambient conditions after transfer to a conventional spectrometer, spectra with a signal increase of 4-5 orders of magnitude can be obtained. Since the introduction of dDNP two decades ago, a number of studies have demonstrated the potential of this technique to study dynamic processes, 2;3 including enzymatic 4;5;6;7;8 and chemical reactions involved in biological processes.