• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata
【24h】

Distal histidine conformational flexibility in dehaloperoxidase from Amphitrite ornata

机译：远端组氨酸构象的灵活性dehaloperoxidase从安菲特律特这种

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The enzyme dehaloperoxidase (DHP) from the terebellid polychaete Amphitrite ornata is a heme protein which has a globin fold but can function as both a hemoglobin and a peroxidase. As a peroxidase, DHP is capable of converting 2,4,6-trihalophenols to the corresponding 2,6-dihaloquinones in the presence of hydrogen peroxide. As a hemoglobin, DHP cycles between the oxy and deoxy states as it reversibly binds oxygen for storage. Here, it is reported that the distal histidine, His55, exhibits conformational flexibility in the deoxy form and is consequently observed in two solvent-exposed conformations more than 9.5 A away from the heme.
机译：这种酶dehaloperoxidase(设计马力)terebellid多毛纲的安菲特律特这种血红素蛋白质球蛋白褶皱但可以功能血红蛋白和过氧化物酶。过氧化物酶,设计马力是转换的能力2、4、6-trihalophenols对应2, 6-dihaloquinones在氢的存在过氧化。氧可逆地结合和脱氧状态氧气用于存储。远端组氨酸、His55展品构象在脱氧的形式,因此灵活性观察到两个solvent-exposed构象超过9.5远离血红素。

著录项

相似文献

  • 外文文献
  • 中文文献
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