Parey, Kristian and Fritz, Guenter and Ermler, Ulrich and Kroneck, Peter M. H. (2013) Conserving energy with sulfate around 100 degrees C - structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus. METALLOMICS, 5 (4). pp. 302-317. ISSN 1756-5901
Full text not available from this repository. (Request a copy)Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | DISSIMILATORY SULFITE REDUCTASE; DESULFOVIBRIO-VULGARIS HILDENBOROUGH; IRON-SULFUR CLUSTER; ADENOSINE 5'-PHOSPHOSULFATE REDUCTASE; CONTAINING HETERODISULFIDE REDUCTASE; ESCHERICHIA-COLI HEMOFLAVOPROTEIN; ELECTRON-PARAMAGNETIC-RESONANCE; BIFUNCTIONAL ATP SULFURYLASE; FE4S4 PROSTHETIC GROUPS; CRYSTAL-STRUCTURE; |
| Subjects: | 500 Science > 540 Chemistry & allied sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie |
| Depositing User: | Petra Gürster |
| Date Deposited: | 27 May 2020 07:07 |
| Last Modified: | 27 May 2020 07:07 |
| URI: | https://pred.uni-regensburg.de/id/eprint/17447 |
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