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

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2013

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Parey, Kristian
Ermler, Ulrich

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https://doi.org/10.1039/c2mt20225e
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Metallomics. 2013, 5(4), pp. 302-317. ISSN 1756-5901. eISSN 1756-591X. Available under: doi: 10.1039/c2mt20225e

Zusammenfassung

Sulfate-reducing bacteria and archaea are important players in the biogeochemical sulfur cycle. ATP sulfurylase, adenosine 5'-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 5'-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.

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570 Biowissenschaften, Biologie

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ISO 690PAREY, Kristian, Günter FRITZ, Ulrich ERMLER, Peter M. H. KRONECK, 2013. Conserving energy with sulfate around 100 °C : structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus. In: Metallomics. 2013, 5(4), pp. 302-317. ISSN 1756-5901. eISSN 1756-591X. Available under: doi: 10.1039/c2mt20225e
BibTex
@article{Parey2013Conse-37737,
  year={2013},
  doi={10.1039/c2mt20225e},
  title={Conserving energy with sulfate around 100 °C : structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus},
  number={4},
  volume={5},
  issn={1756-5901},
  journal={Metallomics},
  pages={302--317},
  author={Parey, Kristian and Fritz, Günter and Ermler, Ulrich and Kroneck, Peter M. H.}
}
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    <dcterms:abstract xml:lang="eng">Sulfate-reducing bacteria and archaea are important players in the biogeochemical sulfur cycle. ATP sulfurylase, adenosine 5'-phosphosulfate reductase and dissimilatory sulfite reductase are the key enzymes in the energy conserving process of SO&lt;sub&gt;4&lt;/sub&gt;&lt;sup&gt;2-&lt;/sup&gt; → H&lt;sub&gt;2&lt;/sub&gt;S reduction. This review summarizes recent advances in our understanding of the activation of sulfate to adenosine 5'-phosphosulfate, the following reductive cleavage to SO&lt;sub&gt;3&lt;/sub&gt;&lt;sup&gt;2-&lt;/sup&gt; and AMP, and the final six-electron reduction of SO&lt;sub&gt;3&lt;/sub&gt;&lt;sup&gt;2-&lt;/sup&gt; 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.</dcterms:abstract>
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