Fritz, Günter and Roth, Annette and Schiffer, Alexander and Buechert, Thomas and Bourenkov, Gleb and Bartunik, Hans D. and Huber, Harald and Stetter, Karl O. and Kroneck, Peter M. H. and Ermler, Ulrich (2002) Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 99 (4). pp. 1836-1841. ISSN 0027-8424
Full text not available from this repository. (Request a copy)Abstract
The iron-sulfur flavoenzyme adenylylsulfate (adenosine 5'-phosphosulfate, APS) reductase catalyzes reversibly the reduction of APS to sulfite and AMP. The structures of APS reductase from the hyperthermophilic Archaeoglobus fulgidus in the two-electron reduced state and with sulfite bound to FAD are reported at 1.6- and 2.5-Angstrom resolution, respectively. The FAD-sulfite adduct was detected after soaking the crystals with APS. This finding and the architecture of the active site strongly suggest that catalysis involves a nucleophilic attack of the N5 atom of reduced FAD on the sulfur atom of APS. In view of the high degree of similarity between APS reductase and fumarate reductase especially with regard to the FAD-binding a-subunit, it is proposed that both subunits originate from a common ancestor resembling archaeal APS reductase. The two electrons required for APS reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD. The exceptionally large difference in reduction potential of these clusters (-60 and -500 mV) can be explained by interactions of the clusters with the protein matrix.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | FUMARATE REDUCTASE; CRYSTAL-STRUCTURE; ELECTRON-TRANSFER; FLAVOCYTOCHROME C(3); ESCHERICHIA-COLI; FERREDOXIN; PROTEIN; ISOALLOXAZINE; METABOLISM; GEOMETRY; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 09 Nov 2021 08:08 |
| Last Modified: | 09 Nov 2021 08:08 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40584 |
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