Sadeghi Sheila J, Fantuzzi Andrea, Gilardi Gianfranco
Department of Human and Animal Biology, University of Turin, Italy.
Biochim Biophys Acta. 2011 Jan;1814(1):237-48. doi: 10.1016/j.bbapap.2010.07.010. Epub 2010 Jul 18.
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.
由于细胞色素P450酶在识别不同生物化合物和外源性化合物方面具有多功能性，因此提高其电化学性能是非常必要的。这项任务带来了一个令人兴奋的挑战，因为它不仅能让我们获得关于这些酶氧化还原特性的基础知识，还为技术和商业应用开辟了机会。事实证明，将这些酶与电极表面连接并通过电化学驱动其催化循环非常困难。几个研究小组最初的尝试包括将这些酶直接固定在电极表面，并省略其氧化还原伙伴以简化电子转移途径。在这些情况下获得的数据通常导致较高的异质电子转移速率，但在可检测的底物周转方面并未成功。当电极和酶都经过改造时，电催化取得了突破，在某些情况下模仿了微粒体酶的自然环境并加入了它们的电子转移伙伴。本文回顾并讨论了关于该主题的最新文献，并强调了导致该研究领域取得前所未有的进展的不同方法。
