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

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

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PAREY, 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. 5(4), pp. 302-317. ISSN 1756-5901. eISSN 1756-591X

@article{Parey2013Conse-37737, title={Conserving energy with sulfate around 100 °C : structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus}, year={2013}, doi={10.1039/c2mt20225e}, 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.} }

Parey, Kristian Conserving energy with sulfate around 100 °C : structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus Kroneck, Peter M. H. 2017-02-27T14:19:03Z Ermler, Ulrich Fritz, Günter 2017-02-27T14:19:03Z Kroneck, Peter M. H. Parey, Kristian 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<sub>4</sub><sup>2-</sup> → H<sub>2</sub>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<sub>3</sub><sup>2-</sup> and AMP, and the final six-electron reduction of SO<sub>3</sub><sup>2-</sup> 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. Ermler, Ulrich eng 2013 Fritz, Günter

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