Fig. 5: Gold-binding properties of the native and synthetic enzymes. | Communications Biology

Fig. 5: Gold-binding properties of the native and synthetic enzymes.

From: Control of carbon monoxide dehydrogenase orientation by site-specific immobilization enables direct electrical contact between enzyme cofactor and solid surface

Fig. 5

a Gold-binding activities of the native CODH-L and of the synthetic constructs as determined by QCM analysis (the arrow indicates the injection of 1 µM enzyme solution). b Comparison of the frequency shift in a. c Changes in the SPR refractive index as a function of time for enzyme adsorption on the gold surface at enzyme concentrations of 12.5, 25, 50, 100, and 200 nM (the solid arrows indicate enzyme injection while the dashed arrows indicate buffer injection). The blue traces represent the global fit of the data to a 1:1 binding model. d Titration curve obtained from plotting the binding response against the enzyme concentration. Key: 1, 2, 3, and 4 refer to CODH-L, CODH-LgbpN, CODH-LgbpC, and CODH-LgbpNC, respectively.

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