Type of Publication: | Journal article |
Publication status: | Published |
Author: | Parey, Kristian; Fritz, Günter; Ermler, Ulrich; Kroneck, Peter M. H. |
Year of publication: | 2013 |
Published in: | Metallomics ; 5 (2013), 4. - pp. 302-317. - ISSN 1756-5901. - eISSN 1756-591X |
Pubmed ID: | 23324858 |
DOI (citable link): | https://dx.doi.org/10.1039/c2mt20225e |
Summary: |
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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Subject (DDC): | 570 Biosciences, Biology |
Bibliography of Konstanz: | Yes |
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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. Available under: doi: 10.1039/c2mt20225e
@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.} }