BACKGROUND Escherichia coli has two L-cysteine biosynthetic pathways; one is synthesized from O-acetyl L-serine (OAS) and sulfate by L-cysteine synthase (CysK), and another is produced via S-sulfocysteine (SSC) from OAS and thiosulfate by SSC synthase (CysM). SSC is converted into L-cysteine and sulfite by an uncharacterized reaction. As thioredoxins (Trx1 and Trx2) and glutaredoxins (Grx1, Grx...

A key step in sulfate assimilation into cysteine is the reduction of sulfite to sulfide by sulfite reductase (SiR). This enzyme is encoded by three genes in the moss Physcomitrella patens. To obtain a first insight into the roles of the individual isoforms, we deleted the gene encoding the SiR1 isoform in P. patens by homologous recombination and subsequently analysed the DeltaSiR1 mutants. Whi...

A thiosulfate reductase from Desulfotomaculum nigrificans has been partially purified by ammonium sulfate fractionation, diethylaminoethylcellulose chromatography, and sucrose density gradient centrifugation. With inner-and outer-labeled (35)S-thiosulfate, the enzyme reduced only the outer sulfur atom to hydrogen sulfide. The enzyme was inhibited by sulfite and also by several sulfhydryl inhibi...

? Multiple Choice Questions Section The Neurosciences Journal includes this section of multiple choice questions as part of its commitment to continuous education and learning in Neurosciences. Experts in various neuroscience specialties are invited to participate with their knowledge and expertise in this section. Neurology, neurosurgery, and other board residents are encouraged to read this s...

In the title compound, C(24)H(34)O(3)S, the dihedral angle between the benzene rings is 84.62 (8)°. In the crystal, inter-molecular C-H⋯O hydrogen bonds link mol-ecules into zigzag chains running parallel to the c axis. The C atoms of two isopropyl groups are disordered over two sets of sites with occupancy ratios of 0.858 (9):0.142 (9) and 0.61 (5):0.39 (5).