L-alpha-glycerophosphate and L-lactate electrodes based on the electrochemical "wiring" of oxidases.
L-alpha-glycerophosphate and L-lactate electrodes based on the electrochemical "wiring" of oxidases.
复制标题
基于氧化酶电化学“线路”的 L-α-甘油磷酸和 L-乳酸电极。
DOI:
10.1021/ac00033a009
复制
发表时间:
1992
影响因子:
7.4
通讯作者:
A. Heller
中科院分区:
文献类型:
--
作者:
I. Katakis;A. Heller
The title electrodes were constructed by coimmobilizing the respective FAD oxidases on solid electrode surfaces with a poly(vinyl pyridine) polymer which was N-derivatized with bromoethylamine and Os(bpy)2Cl2. The redox-polymer-enzyme hydrogels were cross-linked on the electrode surface using poly(ethylene glycol) diglycidyl ether. As in the case of glucose oxidase, the redox polymer acts as an electron relaying "wire" transferring electrons directly from the enzymes' FADH2 centers to the electrode. This transfer competes with the natural process of reoxidation of FADH2 by molecular oxygen. The variation of the response of these electrodes with the atmosphere (N2 or air), pH, and substrate concentration was determined. The pH profile of the electrocatalytic current differs from that of the activity of the free enzymes, exhibiting a broader maximum, shifted to higher pH values. The observed sensitivities and linear ranges are respectively 2 x 10(-2) A M-1 cm-2 and 2.7 mM for L-alpha-glycerophosphate, and 0.3 A M-1 cm-2 and 0.2 mM for L-lactate that may be compared to 2 x 10(-2) A M-1 cm-2 and 10 mM for glucose. The 0-90% response time for all electrodes is 1 s or less.
影响因子:
1.3
作者:
Pietrzyk,DJ;Rigas,PG;Yuan,DX
通讯作者:
Yuan,DX
影响因子:
2.9
作者:
Stankovich,M;Fox,B
通讯作者:
Fox,B
DOI:
--
发表时间:
1986
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Claiborne,A
通讯作者:
Claiborne,A