Structure and function of the bacterial bc1 complex:: Domain movement, subunit interactions, and emerging rationale engineering attempts
Structure and function of the bacterial bc1 complex:: Domain movement, subunit interactions, and emerging rationale engineering attempts
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DOI：
10.1023/a:1005428014548
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发表时间：
1999-06-01
影响因子：
3
通讯作者：
Daldal, F
中科院分区：
文献类型：
--
作者：
Darrouzet, E;Valkova-Valchanova, M;Daldal, F
泛醇：细胞色素c氧化还原酶或bc（1）复合物是呼吸和光合电子传递的关键组分，并有助于形成ATP合成所必需的电化学梯度。许多细菌都有一个bc（1）复合体，它由三个氧化还原活性亚基组成，含有两个b型血红素、一个c型血红素和一个[2Fe-2S]簇作为辅基。光合细菌如红细菌为研究这种酶的功能和结构提供了强有力的模型，并被广泛应用。近年来，自发突变体和定点突变体及其回复突变体的广泛应用，新的抑制剂，在不同物种中发现这种酶的天然变体，以及在适合遗传操作的物种中设计新的bc（1）复合物，为我们提供了关于这种重要酶的功能机制，亚基相互作用性质和组装的丰富信息。最近对不同晶体形式的各种线粒体bc（1）复合物结构的解析巩固了以前的发现，为我们的知识增加了原子尺度的精确度，并提出了新的问题，例如在Q（o）位点催化过程中Rieske Fe-S蛋白亚基的可能运动。本文简要回顾了近几年来利用细菌bc（1）复合物进行的研究，并提到了这一令人兴奋的领域正在进行的研究和未来的挑战。
The ubiquinol: cytochrome c oxidoreductase, or the bc(1) complex, is a key component of both respiratory and photosynthetic: electron transfer and contributes to the formation of an electrochemical gradient necessary for ATP synthesis. Numerous bacteria harbor a bc(1) complex comprised of three redox-active subunits, which bear two b-type hemes, one c-type heme, and one [2Fe-2S] cluster as prosthetic groups. Photosynthetic bacteria like Rhodobacter species provide powerful models for studying the function and structure of this enzyme and are being widely used. In recent years, extensive use of spontaneous and site-directed mutants and their revertants, new inhibitors, discovery of natural variants of this enzyme in various species, and engineering of novel bc(1) complexes in species amenable to genetic manipulations have provided us with a wealth of information on the mechanism of function, nature of subunit interactions, and assembly of this important enzyme. The recent resolution of the structure of various mitochondrial bc(1) complexes in different crystallographic forms has consolidated previous findings, added atomic-scale precision to our knowledge, and raised new issues, such as the possible movement of the Rieske Fe-S protein subunit during Q(o) site catalysis. Here, studies performed during the last few years using bacterial bc(1) complexes are reviewed briefly and ongoing investigations and future challenges of this exciting field are mentioned.