The effect of the electron's spins on the reaction of D-glucose oxidase with D- and L-glucose was investigated by adsorbing the enzyme on a ferromagnetic substrate. The results are consistent with the chiral-induced spin selectivity effect resulting from the improved fidelity of the electron transfer due to the coupling of the linear momentum of the electrons and their spin.

Abstract

The reaction of D-glucose oxidase (GOx) with D- and L-glucose was investigated using confocal fluorescence microscopy and Hall voltage measurements, after the enzyme was adsorbed as a monolayer. By adsorbing the enzyme on a ferromagnetic substrate, we verified that the reaction is spin dependent. This conclusion was supported by monitoring the reaction when the enzyme is adsorbed on a Hall device that does not contain any magnetic elements. The spin dependence is consistent with the chiral-induced spin selectivity (CISS) effect; it can be explained by the improved fidelity of the electron transfer process through the chiral enzyme due to the coupling of the linear momentum of the electrons and their spin. Since the reaction studied often serve as a model system for enzymatic activity, the results may suggest the general importance of the spin-dependent electron transfer in bio-chemical processes.