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Regulation of Glucose Oxidase Activity through Interaction with Fullerene Derivatives
Author(s) -
Gao Yunyan,
Wang Zhongli,
Ou Zhize,
Li Yi,
Wang Xuesong,
Yang Guoqiang
Publication year - 2012
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.201180479
Subject(s) - chemistry , glucose oxidase , hydroxymethyl , fullerene , catalysis , residue (chemistry) , stereochemistry , organic chemistry , enzyme
The 2‐(hydroxymethyl)pyridine modified C 60 (PY‐C 60 ) and methoxydiglycol modified C 60 (MDG‐C 60 ) are synthesized using Bingel‐Hirsch reaction and characterized by nuclear magnetic resonance (NMR) and mass spectra. PY‐C 60 and MDG‐C 60 can bind to glucose oxidase (GOx) and quench the fluorescence of tryptophan (Trp) residue in GOx through static mechanism. The conformation of GOx is disturbed after formation of complex with these fullerene derivatives. Kinetic analysis indicates that PY‐C 60 and MDG‐C 60 may affect the catalytic activity of GOx with a partial mixed‐type inhibition mechanism. In the plasma glucose concentration range (3.6–5.2 mmol·L −1 ), PY‐C 60 may significantly accelerate the catalytic velocity of GOx, however, MDG‐C 60 exerts almost no obvious change to the initial velocity of GOx, suggesting that elaborate design of molecular structure of fullerene derivative is very important for regulating the biological activity of fullerene‐enzyme complex.