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By Christiane Dahl, Cornelius G. Friedrich

In nature, sulfur happens in lots of diverse oxidation states and is among the such a lot flexible parts in lifestyles. it truly is a vital part of many vital phone ingredients, equivalent to the amino acids cysteine and methionine, and plenty of sulfur compounds function the foundation for energy-related techniques in prokaryotes. lately, new tools were utilized to review the biochemistry and molecular biology of reactions of the worldwide sulfur cycle, the microorganisms concerned and their body structure, metabolism and ecology. those actions have exposed attention-grabbing new insights for the knowledge of cardio and anaerobic sulfur metabolism.

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By Christiane Dahl, Cornelius G. Friedrich

In nature, sulfur happens in lots of diverse oxidation states and is among the such a lot flexible parts in lifestyles. it truly is a vital part of many vital phone ingredients, equivalent to the amino acids cysteine and methionine, and plenty of sulfur compounds function the foundation for energy-related techniques in prokaryotes. lately, new tools were utilized to review the biochemistry and molecular biology of reactions of the worldwide sulfur cycle, the microorganisms concerned and their body structure, metabolism and ecology. those actions have exposed attention-grabbing new insights for the knowledge of cardio and anaerobic sulfur metabolism.

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The enzyme APSR (cofactors flavin adenine dinucleotide, [4Fe4S]) catalyzes the conversion of APS to sulf ite (S 4+) and AMP, followed by the comple x multicomponent enzyme SIR (cofactors siroheme, [4Fe4S]) which catalyzes the reduction of sulf ite (S 4+) to sulfide (S 2−). In this contrib ution we present the three-dimensional structures of APSR from Archaeoglobus fulgidus and of catalytically rele vant reaction intermediates. In addition, we discuss spectroscopic and structural data of SIR purif ied from this organism.

This energy-rich state becomes relaxed during the attack of APS on the reduced FAD. A relaxed FAD–sulfite adduct is observed in the structure 18 G. Fritz et al. Fig. 1 Left: The adenosine 5 ′-phosphosulfate reductase (APSR) αβ heterodimer from Archaeoglobus fulgidus. The α-subunit, which harbors the flavin adenine dinucleotide (FAD; yellow), is shown in blue; the β-subunit, with the two [4Fe4S] clusters, is shown in red. The substrate-binding channel is illustrated by approximately 35 tightly bound w ater molecules ( green), indicating a strong electrostatic f ield favorable for binding char ged groups (Fritz et al.

As life may have originated in hot environments (Achenbach-Richter et al. 1987), the occurrences of sulfate-reducing prokaryotes among hyperthermophilic archaea and deep-branching thermophilic bacteria indicate an early origin of this process (Dahl and Trüper 2001). 35 billion years ago (Cameron 1982). Dissimilatory sulfate reduction operates under strictly anaerobic conditions and represents an important element within the biogeochemical sulfur cycle (Peck 1959; LeGall and Fauque 1988; Hansen 1994).

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