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

Journal

METALLOMICS
Volume 5, Issue 4, Pages 302-317

Publisher

ROYAL SOC CHEMISTRY
DOI: 10.1039/c2mt20225e

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Funding

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

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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.

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