Jump to main content
Jump to site search

Issue 4, 2013
Previous Article Next Article

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

Author affiliations

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.

Graphical abstract: Conserving energy with sulfate around 100 °C – structure and mechanism of key metal enzymes in hyperthermophilic Archaeoglobus fulgidus

Back to tab navigation

Publication details

The article was received on 08 Nov 2012, accepted on 18 Dec 2012 and first published on 16 Jan 2013


Article type: Minireview
DOI: 10.1039/C2MT20225E
Metallomics, 2013,5, 302-317

  •   Request permissions

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

    K. Parey, G. Fritz, U. Ermler and P. M. H. Kroneck, Metallomics, 2013, 5, 302
    DOI: 10.1039/C2MT20225E

Search articles by author

Spotlight

Advertisements