首页> 外文会议>International Congress of Photosynthesis >CHLOROPLAST F_1-ATPASE: MOLECULAR MECHANISM OF THE PHYTOTOXIN TENTOXIN
【24h】

CHLOROPLAST F_1-ATPASE: MOLECULAR MECHANISM OF THE PHYTOTOXIN TENTOXIN

机译:叶绿体F_1-ATPase:植物毒素Tentoxin的分子机制

获取原文

摘要

F_0F_1 ATP synthases located in the energy transducing membranes of bacteria, mitochondria and chloroplasts catalyse ATP synthesis and ATP hydrolysis coupled with transmembrane proton transport. The FoFpholoenzymes consist of an extra-membranous catalytic F_1 domain containing five different polypeptides in a stoichiometry of alpha_3beta_3gamma delta epsilon and a membrane intrinsic F_0 domain, composed of subunits a, b and c which mediate proton transfer across the membrane. Structure and molecularmechanism of the membrane extrinsic F_1 domain have been solved with the mitochondrial, bacterial and chloroplast enzymes (Abrahams et al 1994, Bianchet et al 1998, Stock et al 1999, Shirakihara et al 1997, Groth & Pohl 2001). But a detailed structure ofthe membrane embedded F_0 domain which is expected to provide molecular details on the mechanism of proton transfer and energy coupling is still unknown.
机译:F_0F_1 ATP合成酶位于细菌的能量转换膜中,线粒体和叶绿体催化ATP合成和ATP水解与跨膜质子传输。 FEFHOLOEMES由含有五种不同多肽的含有五种不同多肽的常膜催化F_1结构域组成,其由亚基A,B和C组成的亚α_3beta_3gammaδε和C域,其在膜上介导质子转移。用线粒体,细菌和叶绿体酶(Abrahams等,Bianchet等1998,Stock et al 1999,Shirakihara等,Shirakihara等,Grothihara et al 1997,Groth和Pohl 2001)解决了膜外形F_1结构域的结构和分子机制。但是膜嵌入式F_0结构域的详细结构,预计将提供关于质子转移和能量耦合机制的分子细节仍然未知。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号