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  Conserving energy with sulfate around 100 °C - structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus

Parey, K., Fritz, G., Ermler, U., & Kroneck, P. M. H. (2013). Conserving energy with sulfate around 100 °C - structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus. Metallomics, 5(4), 302-317. doi:10.1039/c2mt20225e.

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 Creators:
Parey, Kristian1, Author           
Fritz, Günter2, Author
Ermler, Ulrich1, Author           
Kroneck, Peter M. H.3, Author
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Department of Neuropathology, University of Freiburg, 79106 Freiburg, Germany , ou_persistent22              
3Department of Biology, University of Konstanz, 78457 Konstanz, Germany , ou_persistent22              

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 Abstract: 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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Language(s): eng - English
 Dates: 2012-11-082012-12-182013-01-162013-04
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/c2mt20225e
PMID: 23324858
 Degree: -

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Title: Metallomics
  Alternative Title : Metallomics
Source Genre: Journal
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Pages: - Volume / Issue: 5 (4) Sequence Number: - Start / End Page: 302 - 317 Identifier: -