...
首页> 外文期刊>Angewandte Chemie >The Dinuclear Cu_A Center in Cytochrome c Oxidase and N_2O Reductase-- A Metal-Metal Bond in Biology?
【24h】

The Dinuclear Cu_A Center in Cytochrome c Oxidase and N_2O Reductase-- A Metal-Metal Bond in Biology?

机译:细胞色素c氧化酶和N_2O还原酶中的双核Cu_A中心-生物中的金属键吗?

获取原文
获取原文并翻译 | 示例
   

获取外文期刊封面封底 >>

       

摘要

Neighboring metal centers that cooperate functionally in proteins are bridged predominantly by O, N, or S donor lig-ands. In special cases (such as in, for example, deoxyhemo-cyanin. an oxygen transport protein of molluscs and arthropods that can bindO_2 side-on), the metal centers (here Cu') can be held without additional bridging at a "nonbonding" distance of d> 3.5 A by the protein framework. Recently a direct metal-metal bond in biology was postulated for the first time for the dinuclear Cu_A center in a water-soluble protein domain of the cytochrome c oxidase of Bacillus suhiilis; this proposal was based on the results of new EXAFS measurements (EXAFS = extended X-ray absorption fine structure) and their interpretation in comparison with results from a model compound.
机译:在蛋白质中功能上协作的相邻金属中心主要被O,N或S供体配体桥接。在特殊情况下(例如,在脱氧血蓝蛋白中,一种可以与O_2侧向结合的软体动物和节肢动物的氧转运蛋白),金属中心(此处为Cu')可以保持不变,而无需在“非结合”处桥接。蛋白质框架的距离d> 3.5A。最近,首次在生物学中首次提出了双核Cu_A中心在suacilis芽孢杆菌细胞色素c氧化酶的水溶性蛋白结构域中的直接金属-金属键。该建议基于新的EXAFS测量结果(EXAFS =扩展的X射线吸收精细结构),并与模型化合物的结果进行了比较。

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