4.4 Review

Conserving energy with sulfate around 100 °C - structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus

期刊

METALLOMICS
卷 5, 期 4, 页码 302-317

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/c2mt20225e

关键词

-

资金

  1. Max-Planck Society
  2. Deutsche Forschungsgemeinschaft
  3. University of Konstanz

向作者/读者索取更多资源

Sulfate-reducing bacteria and archaea are important players in the biogeochemical sulfur cycle. ATP sulfurylase, adenosine 50-phosphosulfate reductase and dissimilatory sulfite reductase are the key enzymes in the energy conserving process of SO42- -> H2S reduction. This review summarizes recent advances in our understanding of the activation of sulfate to adenosine 50-phosphosulfate, the following reductive cleavage to SO32- and AMP, and the final six-electron reduction of SO32- to H2S in the hyperthermophilic archaeon Archaeoglobus fulgidus. Structure based mechanisms will be discussed for these three enzymes which host unique metal centers at their catalytic sites.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.4
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据