期刊
PHYSICA STATUS SOLIDI A-APPLICATIONS AND MATERIALS SCIENCE
卷 207, 期 9, 页码 2073-2077出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/pssa.201000043
关键词
cytochrome c; diamond; protein adsorption; surface termination
The adsorption and conformational state of the electron transfer protein cytochrome c (cyt c) on flat, boron doped polycrystalline diamond electrodes was investigated using electrochemical techniques and atomic force microscopy (AFM). An electrochemical reduction wave from the adsorbed protein was identified as oxygen reduction, which is catalysed by the deformed heme redox centre of cyt c. We show that this catalytic activity only occurs after partial denaturation of cyt c. Therefore the reduction peak was used for characterization of the conformational state of adsorbed cyt c. AFM characterizations with molecular resolution show different conformational states of cyt c on diamond surfaces ranging from native to denaturated. Both applied techniques indicate that hydrophobic hydrogenated diamond tends to denaturate cyt c upon adsorption, while wet chemically oxidized diamond surfaces can provide extensive but non-denaturating cyt c adsorption. The conformation and orientation of cyt c on wet chemically oxidized diamond is beneficial for the electron transfer between the protein redox centre and the diamond electrode even in the presence of oxygen. (C) 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
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