A STUDY OF THE KINETICS OF THE REACTION BETWEEN FERROCENE MONOCARBOXYLIC ACID AND GLUCOSE-OXIDASE USING THE ROTATING-DISC ELECTRODE
A STUDY OF THE KINETICS OF THE REACTION BETWEEN FERROCENE MONOCARBOXYLIC ACID AND GLUCOSE-OXIDASE USING THE ROTATING-DISC ELECTRODE
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DOI：
10.1016/0022-0728(95)04173-8
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发表时间：
1995-11-01
影响因子：
4.5
通讯作者：
PRATT, KFE
中科院分区：
文献类型：
--
作者：
BARTLETT, PN;PRATT, KFE
本文介绍了用旋转圆盘电极对葡萄糖/葡萄糖氧化酶/二茂铁单羧酸体系进行研究的结果。在广泛的实验条件下（转速、酶、介质和底物浓度）进行的实验结果与Albery等人提出的理论模型进行了比较。化学。， 323（1992）。在大多数可行的实验条件范围内，实验结果与理论结果吻合良好，该方法是测定酶和介质反应速率的好方法。在酶底物动力学限速的情况下，由于底物浓度极化的影响，数据的正确解释更加困难。本文描述了一种克服这一问题的方法。本文所描述的实验技术和分析方法应普遍适用于介导酶反应的均相动力学研究。
In this paper we present the results of a study of the glucose\glucose oxidase\ferrocene monocarboxylic acid system using the rotating-disc electrode. The results of experiments carried out over a wide range of experimental conditions (rotation speed, enzyme, mediator and substrate concentration) are compared with the theoretical model presented by Albery et al. (J. Electroanal. Chem., 323 (1992) 77). Good agreement between the experiments and theory is demonstrated for most of the available range of experimental conditions, and the method is shown to be a good one for the determination of the rate of reaction of the enzyme and mediator. In the case where the enzyme substrate kinetics are rate limiting it is shown that the correct interpretation of the data is more difficult because of the effects of concentration polarization of the substrate. An approach to overcoming this problem is described. The experimental techniques and analysis described in this paper should be generally applicable to studies of the homogeneous kinetics of mediated enzyme reactions.