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Photochemical and Molecular Dynamics Studies of Halide Binding in Flavoenzyme Glucose Oxidase

Von Wiley-VCH zur Verfügung gestellt

Compared with the halide-free GOX, Cl binding results in disappearance of fluorescence. By contrast, F binding leads to less efficient, and kinetically more homogeneous, fluorescence quenching. Such contrasting effects are rationalized by the differences in the binding behavior of F and Cl to the protein active site.


Glucose oxidase (GOX), a characteristic flavoprotein oxidase with widespread industrial applications, binds fluoride (F) and chloride (Cl). We investigated binding properties of halide inhibitors of GOX through time-resolved spectral characterization of flavin-related photochemical processes and molecular dynamic simulations. Cl and F bind differently to the protein active site and have substantial but opposite effects on the population and decay of the flavin excited state. Cl binds closer to the flavin, whose excited-state decays in <100 fs due to anion-π interactions. Such interactions appear absent in F binding, which, however, significantly increases the active-site rigidity leading to more homogeneous, picosecond fluorescence decay kinetics. These findings are discussed in relation to the mechanism of halide inhibition of GOX by occupying the accommodation site of catalytic intermediates and increasing the active-site rigidity.

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