Why is mno2 an enzyme

Abstract Certain nano-scale metal oxides exhibiting the intrinsic enzyme-like reactivity had been used for environment monitoring. Introduction In recent years, considerable attention has been paid to the applications of artificial nanomaterials as nanozymes in mimicking the intrinsic catalytic function of natural enzymes due to their unique structural, electrical, and optical properties, as well as remarkable catalytic activities [ 1 — 3 ]. Materials and Methods 2. Figure 1. Figure 2.

Figure 3. Figure 4. Figure 5. Studies of kinetic reaction parameters K m and. Figure 6. Figure 7. Role of metal ions i. Figure 8. Linear correlation between the oxidase-like activity of nano-MnO 2 and the logarithmic value of metal ion concentration Log C. Figure 9. UV-Vis differential absorbance spectra DAS calculated on the basis of the data recorded at different metal ion concentrations 0, 0. Table 1. Analytical results for the detection of metal ion-contaminated water samples by MnO 2 nanozyme-2,6-DMP detecting systems.

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This will lead to some parts of our website to not work properly or at all. Turn on javascript for best performance. Glucose oxidation by GOx produces H 2 O 2 , which rapidly decomposes the nanosheets and reduces their absorption. This direct approach for monitoring glucose oxidation enables simpler, real time kinetics analysis compared to methods that employ additional enzymes.

Using this approach, the present study confirms that GOx kinetics is consistent with the Michaelis—Menten MM model, and reveals that the MM constant increases by an order of magnitude with increasing buffer concentration.

Since larger MM constants imply higher enzyme substrate concentrations are required to achieve the same rate of product formation, increasing MM constants imply decreasing enzyme performance. These results demonstrate the facility of using MnO 2 nanosheets to study GOx kinetics and, given the widespread applications of enzymes with buffers, the important sensitivity of enzyme—buffer systems on buffer concentration.

Singh, U. Ungku Faiz, S. Gravelsins, Y. Suganuma, N. Kotoulas, M. Croxall, A. Khan-Trottier, C. Goh and A. Dhirani, Nanoscale Adv. This article is licensed under a Creative Commons Attribution 3.

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