Austrian Institute of Technology GmbH, AIT, Donau-City Str. 1, 1220 Vienna, Austria.
Metallomics. 2011 Jun;3(6):619-27. doi: 10.1039/c0mt00083c. Epub 2011 May 4.
Potentiometric titrations of the cytochrome c oxidase (CcO) immobilized in a biomimetic membrane system were followed by two-dimensional surface-enhanced IR absorption spectroscopy (2D SEIRAS) in the ATR-mode. Direct electron transfer was employed to vary the redox state of the enzyme. The CcO was shown to undergo a conformational transition from a non-activated to an activated state after it was allowed to turnover in the presence of oxygen. Differences between the non-activated and activated state were revealed by 2D SEIRA spectra recorded as a function of potential. The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer.
采用二维表面增强红外吸收光谱(2D SEIRAS)在衰减全反射(ATR)模式下对固定在仿生膜系统中的细胞色素 c 氧化酶(CcO)进行了电位滴定。直接电子转移用于改变酶的氧化还原状态。结果表明,CcO 在有氧存在的情况下发生周转后,会从非激活状态转变为激活状态。通过记录作为电位函数的二维 SEIRA 光谱,可以揭示非激活状态和激活状态之间的差异。激活状态的特点是相关跃迁的数量增加,以及与电子转移相关的氨基酸数量增加。