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  Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-Å resolution

Fritz, G., Roth, A., Schiffer, A., Buchert, T., Bourenkov, G., Bartunik, H. D., et al. (2002). Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-Å resolution. Proceedings of the National Academy of Sciences of the United States of America, 99(4), 1836-1841. doi:10.1073/pnas.042664399.

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 Creators:
Fritz, Günther1, Author
Roth, Annette2, Author           
Schiffer, Alexander3, Author
Buchert, Thomas3, Author
Bourenkov, Gleb4, Author
Bartunik, Hans D.4, Author
Huber, Harald5, Author
Stetter, Karl O.5, Author
Kroneck, Peter M. H.3, Author
Ermler, Ulrich2, Author           
Affiliations:
1Biochemisches Institut, Winterthurerstrasse 190, Universität Zürich, CH-8057 Zürich, Switzerland, ou_persistent22              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Fachbereich Biologie, Mathematisch-Naturwissenschaftliche Sektion, Universität Konstanz, Fach M665, 78457 Konstanz, Germany, ou_persistent22              
4Max-Planck Arbeitsgruppe für Strukturelle Molekularbiologie, 22603 Hamburg, Germany, ou_persistent22              
5Lehrstuhl für Mikrobiologie und Archaeenzentrum, Universität Regensburg, 93053 Regensburg, Germany, ou_persistent22              

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Free keywords: Fumarate reductase ; Crystal-structure ; Electron-transfer ; Flavocytochrome c(3) ; Escherichia-coli ; Ferredoxin ; Protein ; Isoalloxazine ; Metabolism ; Geometry ; Reductase
 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. [References: 38]

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Language(s): eng - English
 Dates: 2001-08-092001-12-122002-02-122002-02-19
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.042664399
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 99 (4) Sequence Number: - Start / End Page: 1836 - 1841 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230