By Christiane Dahl, Cornelius G. Friedrich
In nature, sulfur happens in lots of diverse oxidation states and is without doubt one of the such a lot flexible parts in lifestyles. it truly is a vital part of many vital mobilephone parts, corresponding to the amino acids cysteine and methionine, and lots of sulfur compounds function the root for energy-related strategies 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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Additional resources for Microbial sulfur metabolism
Dt. psychrophila and A. fulgidus have hydrogenases and formate dehydrogenases with a cytochrome b membrane sub unit, which transfers electrons to the menaquinone pool. , which include a cytochrome c subunit also belonging to the cytochrome c3 family (Matias et al. 2005; Fig. 1). The c ytochrome c sub units of three of these comple xes, 3 Respiratory Membrane Complexes of Desulfovibrio 31 HmcA, 9HcA and TmcA, ha ve been isolated and characterized, and recently the Tmc complex was also isolated. It is still not clear whether these three comple xes transfer electrons to the menaquinone pool and/or directly to the c ytoplasm for reduction of sulf ate.
1). The α-subunit harbors the FAD prosthetic group and can be di vided into three domains. This architecture classifies APSR as member of the fumarate reductase family (Lancaster 2003). The β-subunit consists of a bacterial ferredoxin-type se gment with tw o [4Fe4S] clusters, a three-stranded antiparallel β-sheet and a tail with a length of 50 Å (Fig. 2). The global part of the β-subunit is embedded into a broad cleft of the α-subunit, while its long tail wraps around the α-subunit (Fig. 1). The reaction of APSR consists of an electron transfer step and the reducti ve cleavage of the ester moiety of APS.
The electron paramagnetic resonance spectrum of the oxidized comple x confirms the presence of the TmcB FeS center with similar characteristics to that of the D. desulfuricans DsrK and assigned to a [4Fe4S] 3+ center. TpIIc3 (TmcA) is ef ficiently reduced by the pair hydrogenase/ TpIc3 (Matias et al. 2005). Reduction of the Tmc comple x with H 2 and hydrogenase/ TpIc3 led to almost complete reduction of all the redox centers. This supports the prediction that the Tmc complex is a transmembrane conduit for electrons resulting fromperiplasmic hydrogen oxidation.