Abstract
The reactivity of tyrosinase adsorbed on nanogold bound with 4,4′-bis(methanethiol)biphenyl monolayer self-assembled on a gold disk with catechol in a dipolar aprotic solvent, acetonitrile (AN), was studied by cyclic voltammetric and amperometric methods. Tyrosinase exhibited characteristics of a Michaelis-Menten kinetic mechanism. The tyrosinase attached to the nanogold continued to react with substrates in AN even when the water content was lower than 0.01 w/w%. The apparent Michaelis-Menten constant Km of tyrosinase for catechol is 5.5 ± 0.4 mM (n = 5).
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Nakamura, T., Ren, J., Zhu, Km. et al. Application of the Nanogold-4,4′-bis(methanethiol)biphenyl Modified Gold Electrode to the Determination of Tyrosinase-Catechol Reaction Kinetics in Acetonitrile. ANAL. SCI. 22, 1261–1264 (2006). https://doi.org/10.2116/analsci.22.1261
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DOI: https://doi.org/10.2116/analsci.22.1261