Conformational changes in the cytochrome b6f complex induced by inhibitor binding
Conformational changes in the cytochrome b6f complex induced by inhibitor binding
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DOI：
10.1074/jbc.275.18.13195
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发表时间：
2000-05-05
影响因子：
4.8
通讯作者：
Breyton, C
中科院分区：
文献类型：
--
作者：
Breyton, C
bc型复合体Q(o)位点的抑制因子stmatellin的结合已被证明可诱导呼吸道bc(1)复合体中Rieske蛋白的大构象变化(Kim， H., Xia， D., Yu， C. A.， A. M., Kachurin， A. M., Zhang， L., Yu， L., and Deisenhofer， J. (1998) Proc. Natl.。学会科学。《美国法典》95,8026-8033；Iwata， S., Lee， J. W., Okada， K., Lee， J. K., Iwata， M., Rasmussen， B., Link， T. A., Ramaswamy， S.，和clap， B. K. (1998) Science 281, 64-71；张志强，黄磊，Shulmeister， V. M, Chi， Y. I, Kim， K. K., Hung， L. W., Crofts， A. R., Berry， E. A., Kim， S. A（1998）《自然》，392,677-684)。这样的运动似乎是将电子从膜溶喹啉转移到细胞色素c的膜外血红素所必需的(1)。为了了解相关的光合作用b(6)f复合体是否也发生了类似的变化，我们利用电子晶体学研究了柱头藻素与真核生物b(6)f复合体结合的影响。比较有或没有柱头蛋白制备的薄三维晶体的投影图，无论是阴性染色还是包埋在葡萄糖中，揭示了与bc(1)复合物相似的运动类型，并表明跨膜区域发生了构象变化。
Binding of stigmatellin, an inhibitor of the Q(o) site of the bc-type complexes, has been shown to induce large conformational changes of the Rieske protein in the respiratory bc(1) complex (Kim, H., Xia, D., Yu, C. A., Xia, J. Z., Kachurin, A. M., Zhang, L., Yu, L., and Deisenhofer, J. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 8026-8033; Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., and clap, B. K. (1998) Science 281, 64-71; Zhang, Z., Huang, L., Shulmeister, V. M., Chi, Y. I., Kim, K. K., Hung, L. W., Crofts, A. R., Berry, E. A., and Kim, S. a (1998) Nature 392, 677-684). Such a movement seems necessary to shuttle electrons from the membrane-soluble quinol to the extramembrane heme of cytochrome c(1). To see whether similar changes occur in the related photosynthetic b(6)f complex, we have studied the effect of the binding of stigmatellin to the eukaryotic b(6)f complex by electron crystallography. Comparison of projection maps of thin three-dimensional crystals prepared with or without stigmatellin, and either negatively stained or embedded in glucose, reveals a similar type of movement to that observed in the bc(1) complex and suggests also the occurrence of conformational changes in the transmembrane region.