Dynamic and structural properties of glucose oxidase enzyme |
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| Authors: | Ahmed Haouz Charles Twist Christian Zentz Patrick Tauc B Alpert |
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| Institution: | (1) Laboratoire de Biologie Physico-Chimique, Université Denis Diderot, 2 Place Jussieu, F-75257 Paris, France (e-mail: bea@ccr.jussieu.fr), FR;(2) LURE and Laboratoire de Biochimie Moléculaire et Cellulaire, Université Paris 11, Orsay, France, FR |
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| Abstract: | The catalytic oxidation of β-D-glucose by the enzyme glucose oxidase involves a redox change of the flavin coenzyme. The structure and the dynamics of
the two extreme glucose oxidase forms were studied by using infrared absorption spectroscopy of the amide I′ band, tryptophan
fluorescence quenching and hydrogen isotopic exchange. The conversion of FAD to FADH2 does not change the amount of α-helix present in the protein outer shell, but reorganises a fraction of random coil to β-sheet structure. The dynamics of the protein interior vary with the redox states of the flavin without affecting the motions
of the structural elements near the protein surface. From the structure of glucose oxidase given by X-ray crystallography,
these results suggest that the dynamics of the interface between the two monomers are involved in the catalytic mechanism.
Received: 27 December 1996 / Accepted: 18 July 1997 |
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| Keywords: | Aspergillus niger Glucose oxidase FTIR Proton exchange Secondary structure Protein dynamics |
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