Abstract
A critical issue in bioelectrochemical applications that use electrodes modified by Single Wall Carbon Nanotubes (SWCNTs) is to ensure high activity of the catalytic site of an immobilized enzyme protein interacting with nanomaterials. Since Flavin Adenine Dinucleotide (FAD), a coenzyme of glucose oxidase (GOx), is the active center of the catalytic site, conformation of which could determine the activity of enzyme, it is important to understand the dynamic mechanism of its conformational mobility while GOx is adsorbed on SWCNTs with multiple orientations. However, this dynamic mechanism still remains unclear at the atomic level due to the coenzyme being embedded in the apo-GOx and the limitations of appropriate experimental methods. In this study, a molecular dynamics (MD) simulation was performed to investigate the conformational mobility mechanism of the coenzyme. The trajectory and the interaction energy clearly indicate that the adsorption of GOx onto SWCNTs plays an important role in the conformational mobility of the coenzyme, and its mobility is greatly affected by the distribution of water molecules due to it being hydrophobic.
Highlights
Glucose oxidase (GOx) electrodes have been extensively studied as a foundation for constructing biosensors, biomedical devices, enzymatic bioreactors and biofuel cells [1,2,3,4,5,6]
It had been found that GOx complex and Flavin Adenine Dinucleotide (FAD) coenzymes can spontaneously adsorb onto annealed carbon nanotubes with an armchair chirality to improve their bioelectrochemical performance respectively while these complexes are cast onto glassy carbon electrodes (GCEs) [5, 13,14]
In order to recognize what are about the change of activity with GOx complex adsorbed on SWCNTs, it would be worthy of exploring the conformational mobility mechanism of FAD coenzyme while GOx complex is non-covalently adsorbed on SWCNTs with multiple orientations
Summary
Glucose oxidase (GOx) electrodes have been extensively studied as a foundation for constructing biosensors, biomedical devices, enzymatic bioreactors and biofuel cells [1,2,3,4,5,6]. In order to recognize what are about the change of activity with GOx complex adsorbed on SWCNTs, it would be worthy of exploring the conformational mobility mechanism of FAD coenzyme while GOx complex is non-covalently adsorbed on SWCNTs with multiple orientations. Of cause, those experiments on SWCNT-modified electrodes have proven to be an essential experimental base for gaining a fundamental understanding of biological redox reactions and for evaluating potential denaturation mechanisms due to the interaction with SWCNTs [13,14]. Based on previous research performed by our group [16,17,18,19], and could help us to make further clear some critical issues about the immobilization of enzyme with SWCNTs in bioelectrochemical applications
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