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.
Original language | English |
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Article number | e202400033 |
Journal | ChemPhysChem |
Volume | 25 |
Issue number | 10 |
Early online date | 27 Feb 2024 |
DOIs | |
Publication status | Published - 17 May 2024 |
Funding
We acknowledge partial support by the U.S. Air Force Office of Scientific Research Grant No. FA9550-21-1-0418 and from the Estate of Rena G. Moses and the Laurie Kayden Foundation. Publisher Copyright: © 2024 The Authors. ChemPhysChem published by Wiley-VCH GmbH.
All Science Journal Classification (ASJC) codes
- Atomic and Molecular Physics, and Optics
- Physical and Theoretical Chemistry