Surface enhanced Raman scattering study of horse heart cytochrome c at a silver electrode in the presence of bis(4-pyridyl)disulfide and purine
Surface enhanced Raman scattering study of horse heart cytochrome c at a silver electrode in the presence of bis(4-pyridyl)disulfide and purine
复制标题
双(4-吡啶基)二硫化物和嘌呤存在下银电极上马心细胞色素 c 的表面增强拉曼散射研究
DOI:
10.1016/s0022-0728(84)80371-x
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发表时间:
1984
影响因子:
4.5
通讯作者:
K. Yasukouchi
中科院分区:
文献类型:
--
作者:
I. Taniguchi;M. Iseki;H. Yamaguchi;K. Yasukouchi
Direct, rapid electron-transfer between electrodes and c-type cytochromes has been the subject of current interest in bioelectroanalytical chemistry [1]. In the presence of 4, 4'-bipyridine, which was the first promoter found by Eddowes and Hill [2], the acceleration of the rate of heterogeneous electrontransfer of cytochrome c at gold [3--6] and platinum [7] electrodes has been observed. Recently, we have shown [8] that a bis (4-pyridyl) disulfide (PySSPy) modified gold electrode works as a suitable electrode for rapid electron-transfer of cytochrome c without any promoter or mediator in the solution, although PySSPy itself is electro-inactive at the potentials of interest. More recently, we have reported that purine and some of its derivatives are also effective as new promoters for cytochrome c [9].However, the origin of the enhancement of electron-transfer kinetics is not yet well understood. Hill and co-workers [3--6] suggested that the electrontransfer of cytochrome c takes place on the promoter-adsorbed conducting layer, while Hinnen et al.[10] claimed, from the results of spectroreflectance measurement, that cytochrome c and 4, 4'-bipyridine are adsorbed together on a gold electrode and the strong interaction between cytochrome c and the promoter is questionable. Very recently, Cotton et al.[11] have reported, by surface enhanced Raman scattering (SERS) measurement, that an Ag (I)--4, 4'-bipyridine complex is formed on the Ag electrode which facilitates the electron-transfer of cytochrome c at the electrode. However, to date, little is known about the surface profile of a promoter-modified electrode. To understand the interaction between cytochrome c and a promoter-modified electrode better, it is essential to clarify the structure of the promoter-adsorbed surface of the electrode. For this purpose, the SERS measurement is one of the most powerful techniques. In fact, SERS spectra of cytochrome c in the presence of PySSPy and purine provided interesting information about the adsorbed species on the electrode.