Inorganic Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, Oxford, OX1 3QR, UK.
Chem Commun (Camb). 2012 Feb 1;48(10):1400-9. doi: 10.1039/c1cc15871f. Epub 2011 Nov 7.
This article reviews recent developments in spectroscopic analysis of electrode-immobilised enzymes under direct, unmediated electrochemical control. These methods unite the suite of spectroscopic methods available for characterisation of structural, electronic and coordination changes in proteins with the exquisite control over complex redox enzymes that can be achieved in protein film electrochemistry in which immobilised protein molecules exchange electrons directly with an electrode. This combination is particularly powerful in studies of highly active enzymes where redox states can be controlled even under fast electrocatalytic turnover. We examine examples in which UV-visible, IR, Raman and MCD spectroscopy have been combined with direct electrochemistry to probe redox-dependent chemistry, and consider future opportunities for 'direct' spectroelectrochemistry of immobilised enzymes.
本文综述了在直接、无中介电化学控制下固定化酶的光谱分析的最新进展。这些方法将可用于蛋白质结构、电子和配位变化特征化的光谱方法与在蛋白质膜电化学中对复杂氧化还原酶进行的精确控制结合在一起，在蛋白质膜电化学中，固定化蛋白质分子可以与电极直接交换电子。这种组合在研究高活性酶时特别强大，在这些酶中，即使在快速电催化转化下，也可以控制氧化还原状态。我们考察了将紫外可见光谱、红外光谱、拉曼光谱和磁圆二色光谱与直接电化学相结合来探测依赖于氧化还原的化学的实例，并考虑了固定化酶的“直接”光谱电化学的未来机遇。
