Neehaul Yashvin, Chen Ying, Werner Carolin, Fee James A, Ludwig Bernd, Hellwig Petra
CNRS-Université de Strasbourg, Strasbourg, France.
Biochim Biophys Acta. 2012 Oct;1817(10):1950-4. doi: 10.1016/j.bbabio.2012.02.027. Epub 2012 Feb 28.
The hydrophobically guided complex formation between the Cu(A) fragment from Thermus thermophilus ba(3) terminal oxidase and its electron transfer substrate, cytochrome c(552), was investigated electrochemically. In the presence of the purified Cu(A) fragment, a clear downshift of the c(552) redox potential from 171 to 111mV±10mV vs SHE' was found. Interestingly, this potential change fully matches complex formation with this electron acceptor site in other oxidases guided by electrostatic or covalent interactions. Redox induced FTIR difference spectra revealed conformational changes associated with complex formation and indicated the involvement of heme propionates. This article is part of a Special Issue entitled: 17th European Bioenergetics Conference (EBEC 2012).
对嗜热栖热菌ba(3)末端氧化酶的铜(A)片段与其电子传递底物细胞色素c(552)之间的疏水引导复合物形成进行了电化学研究。在纯化的铜(A)片段存在的情况下，发现相对于标准氢电极（SHE'），c(552)氧化还原电位从171mV明显下移至111mV±10mV。有趣的是，这种电位变化与其他氧化酶中由静电或共价相互作用引导的该电子受体位点的复合物形成完全匹配。氧化还原诱导的傅里叶变换红外差谱揭示了与复合物形成相关的构象变化，并表明血红素丙酸酯参与其中。本文是名为“第17届欧洲生物能量学会议（EBEC 2012）”的特刊的一部分。
