title: 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 SO4(2-) → H2S reduction. This review summarizes recent advances in our understanding of the activation of sulfate to adenosine 5'-phosphosulfate, the following reductive cleavage to SO3(2-) and AMP, and the final six-electron reduction of SO3(2-) 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.
authors: Max-Planck-Institute of Biophysics, Max-von-Laue-Str. 3, 60438 Frankfurt, Germany.
authors: Kristian
authors: K
authors: Parey
authors: Günter
authors: G
authors: Fritz
authors: Ulrich
authors: U
authors: Ermler
authors: Peter M H
authors: PM
authors: Kroneck
mesh_terms: D019611:Archaeoglobus fulgidus / Q000201:enzymology*; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D008670:Metals / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013431:Sulfates / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D004798:Enzymes; D008670:Metals; D013431:Sulfates