期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1814, 期 1, 页码 237-248出版社
ELSEVIER
DOI: 10.1016/j.bbapap.2010.07.010
关键词
Cytochrome P450; Electrochemistry; Immobilisation; Substrate turnover; Electron transfer; Biotechnology
Improving the electrochemical performance of cytochrome P450 enzymes is highly desirable due to their versatility in the recognition of different biological and xenobiotic compounds. The task poses an exciting challenge because it leads not only to the acquisition of fundamental knowledge on the redox properties of these enzymes, but it also opens opportunities for technological and commercial applications. Interfacing these enzymes to electrode surfaces and electrochemically driving their catalytic cycle has proven to be very difficult. Initial attempts made by several groups included the direct immobilisation of these enzymes on electrode surfaces and omission of their redox partners for simplification of their electron transfer pathway. The data obtained in these cases generally resulted in a high heterogeneous electron transfer rate but without success in terms of detectable substrate turnover. The breakthrough in electrocatalysis has been made when both the electrode and the enzyme have been engineered, in some cases mimicking the natural environment of the microsomal enzymes and the inclusion of their electron transfer partners. This paper reviews and discusses the recent literature on this subject, and highlights the different approaches that have led to an unprecedented advancement of this area of research.(C) 2010 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据