...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of bacteriology >Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme.
【24h】

Characterization of the CO-induced, CO-tolerant hydrogenase from Rhodospirillum rubrum and the gene encoding the large subunit of the enzyme.

机译：表征来自红螺螺旋藻的CO诱导的，耐CO的加氢酶和编码该酶大亚基的基因。

获取原文
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

In the presence of carbon monoxide, the photosynthetic bacterium Rhodospirillum rubrum induces expression of proteins which allow the organism to metabolize carbon monoxide in the net reaction CO + H2O --> CO2 + H2. These proteins include the enzymes carbon monoxide dehydrogenase (CODH) and a CO-tolerant hydrogenase. In this paper, we present the complete amino acid sequence for the large subunit of this hydrogenase and describe the properties of the crude enzyme in relation to other known hydrogenases. The amino acid sequence deduced from the CO-induced hydrogenase large-subunit gene (cooH) shows significant similarity to large subunits of other Ni-Fe hydrogenases. The closest similarity is with HycE (58% similarity and 37% identity) from Escherichia coli, which is the large subunit of an Ni-Fe hydrogenase (isoenzyme 3). The properties of the CO-induced hydrogenase are unique. It is exceptionally resistant to inhibition by carbon monoxide. It also exhibits a very high ratio of H2 evolution to H2 uptake activity compared with other known hydrogenases. The CO-induced hydrogenase is tightly membrane bound, and its inhibition by nonionic detergents is described. Finally, the presence of nickel in the hydrogenase is addressed. Analysis of wild-type R. rubrum grown on nickel-depleted medium indicates a requirement for nickel for hydrogenase activity. However, analysis of strain UR294 (cooC insertion mutant defective in nickel insertion into CODH) shows that independent nickel insertion mechanisms are utilized by hydrogenase and CODH. CooH lacks the C-terminal peptide that is found in other Ni-Fe hydrogenases; in other systems, this peptide is cleaved during Ni processing.
机译：在一氧化碳的存在下，光合作用细菌Rhodospirspirillum rubrum诱导蛋白质的表达，使有机体在净反应CO + H2O-> CO2 + H2中代谢一氧化碳。这些蛋白质包括一氧化碳脱氢酶（CODH）和耐CO的氢化酶。在本文中，我们介绍了该氢化酶大亚基的完整氨基酸序列，并描述了与其他已知氢化酶有关的粗酶的性质。由CO诱导的氢化酶大亚基基因（cooH）推导的氨基酸序列与其他Ni-Fe氢化酶的大亚基显示出显着相似性。最接近的相似性是与大肠杆菌的HycE（相似性为58％，同一性为37％），它是Ni-Fe氢化酶（同功酶3）的大亚基。 CO诱导的氢化酶的性质是独特的。它具有出色的抗一氧化碳抑制能力。与其他已知的氢化酶相比，它还表现出非常高的H2释放与H2吸收活性比率。 CO诱导的加氢酶与膜紧密结合，描述了非离子型去污剂对其的抑制作用。最后，解决了氢化酶中镍的存在。对贫镍培养基上生长的野生型红景天的分析表明，镍对于氢化酶活性的需求。但是，对菌株UR294（镍插入CODH的缺陷的cooC插入突变体）的分析表明，氢化酶和CODH利用了独立的镍插入机制。 CooH缺乏在其他Ni-Fe氢化酶中发现的C末端肽。在其他系统中，该肽在镍加工过程中被裂解。

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