Irreversible and Reversible Deactivation of Bilirubin Oxidase by Urate |
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Authors: | Hyosul Shin Chan Kang Adam Heller |
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Institution: | 1. Department of Chemistry, Research Institute of Physic and Chemistry, Chonbuk National University, Chonju 561‐756, The Republic of Korea;2. Department of Chemical Engineering, The University of Texas, Austin, TX 78712,?USA |
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Abstract: | Oxygen is electroreduced to water on a carbon cathode coated with wired bilirubin oxidase in a pH 7.4 0.15 M NaCl phosphate buffer solution at 37 °C at much lesser polarization than it is on a pure platinum cathode in 0.5 M H2SO4. While the wired bilirubin oxidase cathode operates for over a week in the aerated or oxygenated buffer solution, it is degraded rapidly when in serum. We reported earlier that in the presence of O2 an intermediate product of the electrooxidation of urate, which is a normal serum component, irreversibly damages the wired bilirubin oxidase and also reported that the electrocatalyst is irreversibly damaged, in the absence of urate, when it is brought, by disconnecting the electrode, to the O2/H2O half cell potential at pH 7.4. Here we report that a) dissolved bilirubin oxidase is irreversibly and rapidly damaged by urate in the presence of O2; and b) that the immobilized wired bilirubin oxidase electrocatalyst is not only irreversibly deactivated by urate in the presence of O2 in a few hours, but is initially reversibly deactivated, in 1 min or less, by the urate in the presence of O2. |
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Keywords: | Bioelectrochemistry Oxygen cathode Oxygen electroreduction Wired enzyme Bioelectrocatalyst |
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