Issue 4, 2013

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

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

Article information

Article type
Minireview
Submitted
08 Nov 2012
Accepted
18 Dec 2012
First published
16 Jan 2013

Metallomics, 2013,5, 302-317

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