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          Institute: MPI für Biophysik     Collection: Abt. Molekulare Membranbiologie     Display Documents

ID: 12060.0, MPI für Biophysik / Abt. Molekulare Membranbiologie
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-Å resolution
Authors:Fritz, G.; Roth, A.; Schiffer, A.; Buchert, T.; Bourenkov, G.; Bartunik, H. D.; Huber, H.; Stetter, K. O.; Kroneck, P. M. H.; Ermler, U.
Date of Publication (YYYY-MM-DD):2002
Title of Journal:Proceedings of the National Academy of Sciences of the United States of America
Issue / Number:4
Start Page:1836
End Page:1841
Review Status:not specified
Audience:Experts Only
Abstract / Description: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. [References: 38]
Free Keywords:Fumarate reductase
; Crystal-structure
; Electron-transfer
; Flavocytochrome c(3)
; Escherichia-coli
; Ferredoxin
; Protein
; Isoalloxazine
; Metabolism
; Geometry
; Reductase
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für Biophysik/Abteilung Molekulare Membranbiologie
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