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

@article{Parey2013ConservingEW,
  title={Conserving energy with sulfate around 100 °C--structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus.},
  author={Kristian Parey and Guenter Fritz and Ulrich Ermler and Peter M. H. Kroneck},
  journal={Metallomics : integrated biometal science},
  year={2013},
  volume={5 4},
  pages={
          302-17
        }
}

• Kristian Parey, Guenter Fritz, +1 author Peter M. H. Kroneck
• Published 2013 in Metallomics : integrated biometal science
• DOI:10.1039/c2mt20225e

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 SO4(2-) → H2S reduction. This review summarizes recent advances in our understanding of the activation of sulfate to adenosine 5'-phosphosulfate, the following reductive cleavage to SO3(2-) and AMP, and the final six-electron reduction of SO3(2-) to H2S in… CONTINUE READING

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