Gorlaeus Laboratories, Leiden Institute of Chemistry, Leiden University, The Netherlands.
FEBS J. 2014 Nov;281(21):4892-905. doi: 10.1111/febs.13028. Epub 2014 Sep 26.
It has been demonstrated that the complex of yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP) exists as a delicate equilibrium of a specific, active state and the non-specific, dynamic encounter state. An ortholog of yeast Cc, horse Cc, binds CcP but forms a much more dynamic complex, as demonstrated by NMR spectroscopy. A single conservative mutation of lysine 13 to arginine reduces the dynamics and enhances the specificity. The crystal structure of the stereospecific complex resembles the yeast Cc-CcP complex. In contrast, the K13A mutation increases the dynamic nature of the complex with CcP, showing that specificity in a redox protein complex can depend on the interactions of a single side chain in the binding interface.
已经证明，酵母细胞色素 c（Cc）和细胞色素 c 过氧化物酶（CcP）复合物存在于特定的、活跃状态和非特异性的、动态的相遇状态之间的微妙平衡中。酵母 Cc 的同源物马 Cc 与 CcP 结合，但形成了一个更加动态的复合物，这一点通过 NMR 光谱学得到了证明。单一的保守性赖氨酸 13 突变为精氨酸降低了动力学特性并增强了特异性。立体特异性复合物的晶体结构类似于酵母 Cc-CcP 复合物。相比之下，K13A 突变增加了与 CcP 的复合物的动态性质，表明在氧化还原蛋白复合物中的特异性可以取决于结合界面中单一侧链的相互作用。
