Conformational Mobility of GOx Coenzyme Complex on Single-Wall Carbon Nanotubes

Sensors

Feng Liu¹  Xue-song Ye¹  Tao Wu²  Chang-Tao Wang¹  Jia-wei Shen² 

[1] Collage of Biomedical Engineering & Instrument Science, University of Zhejiang, P.R. China. EMail:;Department of Chemistry, University of Zhejiang, P.R. China. E-Mails:

关键词: Molecular mechanism;    Immobilization;    Conformational mobility;    Embedded coenzyme;   

DOI  :  10.3390/s8128453

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2008 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.