Global ETD Search
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Showing 1 to 8 of 8 for “"Sulfur transfer"”.
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Protein Specificity Dictates Proper Sulfur Transfer in the Biosynthesis of Thio-cofactors in Bacteria
Sulfur-containing biomolecules including iron-sulfur clusters, thio-nucleosides, and other thio-cofactors are critical players in several biological processes. The sulfur element present in these molecules is predominantly originated from L-cysteine through activation by cysteine desulfurases and …
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FUNCTIONAL STUDIES OF THE FE-S CLUSTER BIOGENESIS BY SUF SYSTEM
Iron-Sulfur clusters are important metal cofactors for many enzymes. Bacteria have dedicated systems for the maturation and trafficking of Fe-S clusters. The SUF (Sulfur Utilization Factor) system is the only housekeeping system in Gram-positive bacteria; whereas in Gram-negative bacteria, the SUF …
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Characterization of Fe-S Cluster Assembly On the Sufbc2D Complex
<p>In vivo biogenesis of iron-sulfur (Fe-S) cluster cofactors requires complex biosynthetic machinery to limit release of iron and sulfide, to protect the Fe-S cluster from oxidation, and to target the Fe-S cluster to the correct apo-enzyme. The SufABCDSE pathway for Fe-S cluster assembly in E. …
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Studies of unusual catalysis : a tale of four enzymes from diverse biosynthesis pathways
… MoeZ from Amycolatopsis orientalis is a unique sulfur carrier protein (SCP) activating enzyme that participates in the metabolism of sulfur. Unlike reported pathway specific homologues, MoeZ can activate multiple SCPs from different biosynthesis pathways found in A. orientalis. Herein, the …
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Biochemical and genetic characterization of mercaptopyruvate sulfurtransferase and paralogous putative sulfurtransferases of Escherichia coli
Sulfurtransferases, including mercaptopyruvate sulfurtransferase and rhodanese, are widely distributed in living organisms. Mercaptopyruvate sulfurtransferase and rhodanese catalyze the transfer of sulfur from mercaptopyruvate and thiosulfate, respectively, to sulfur acceptors such as thiols or …
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Organometallic imido, sulfido and oxo complexes of osmium(VI)
Transition metal-mediated oxygen, nitrogen, and sulfur transfer reactions to olefins and acetylenes were reviewed in Chapter 1. The alkylosmium(VI) complexes (Y) (Os(N)(R)$\sb2$Cl$\sb2$), Os(N)(CH$\sb2$SiMe$\sb3)\sb2$Cl, Os(N)(CH$\sb2$SiMe$\sb3)\sb2$Cl(NC$\sb5$H$\sb5)$, Os …
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Characterization of two novel proteins containing the rhodanese homology domain: YgaP and YbbB of Escherichia coli
… some members of this family of proteins show sulfurtransferase activity in vitro, their specific physiological functions remain largely undefined. Fusion of a rhodanese domain to different protein domains of known or unknown functions provides important clues to the diverse roles for these …
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Reaktionen elektrophiler und nucleophiler Schwefeldonoren mit cyclischen Alkenen und Alkinen
… Ausbeute episulfidiert werden. Beim Schwefeltransfer vom Sulten auf 1-Methoxycycloocten entsteht das Produkt einer Insertion des Enolethers in die O-S-Bindung des Sultens in 69 Prozent Ausbeute. Wird das Sulten mit Cyclooctin und einem Äquivalent Trifluoressigsäure oder einer anderen starken …