Larsen R W, Pan L P, Musser S M, Li Z Y, Chan S I
Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
Proc Natl Acad Sci U S A. 1992 Jan 15;89(2):723-7. doi: 10.1073/pnas.89.2.723.
This paper explores the proton pumping function of cytochrome c oxidase [ferrocytochrome-c:oxygen oxidoreductase (EC 1.9.3.1)] based upon redox linkage at the "high-potential" CuB center. A model is proposed that is derived from a redox-linked ligand exchange mechanism previously described for the CuA site. Qualitative analysis of this mechanism indicates that such a mechanism is feasible. However, the relatively short distance between CuB and cytochrome a3 implies that the uncoupling electron transfers are quite facile. In addition, the position of the CuB center with respect to the inner mitochondrial membrane argues against redox linkage at the CuB site.
本文基于“高电位”CuB中心的氧化还原连接,探讨了细胞色素c氧化酶[亚铁细胞色素c:氧氧化还原酶(EC 1.9.3.1)]的质子泵功能。提出了一个模型,该模型源自先前描述的CuA位点的氧化还原连接配体交换机制。对该机制的定性分析表明,这种机制是可行的。然而,CuB与细胞色素a3之间相对较短的距离意味着解偶联电子转移相当容易。此外,CuB中心相对于线粒体内膜的位置不利于在CuB位点进行氧化还原连接。