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Carbon Bond Cleavage (carbon + bond_cleavage)
Selected AbstractsNickel-Catalyzed Regioselective Carbomagnesation of Methylenecyclopropanes through a Site-Selective Carbon,Carbon Bond Cleavage,ANGEWANDTE CHEMIE, Issue 1 2010Jun Terao Dr. Den Ring sprengen: In Gegenwart eines Nickelkatalysators addieren Vinyl- oder Aryl-Grignard-Reagentien unter selektiver C-C-Bindungsspaltung an Methylencyclopropane (siehe Schema). Die Reaktion eröffnet einen neuen Zugang zu substituierten Homoallyl- und Allyl-Grignard-Reagentien. [source] ChemInform Abstract: Ring Opening of Cyclic Vinylogous Acyl Triflates Using Stabilized Carbanion Nucleophiles: Claisen Condensation Linked to Carbon,Carbon Bond Cleavage.CHEMINFORM, Issue 37 2010David M. Jones Abstract Treatment of the cyclic triflates (I) and (VII) with carbanion nucleophiles provides acyclic alkynes bearing 1,3-diketone, ,-keto ester, ,-keto phosphonate, or ,-keto phosphine oxide moieties. [source] ChemInform Abstract: Nickel-Catalyzed Regioselective Carbomagnesation of Methylenecyclopropanes Through a Site-Selective Carbon,Carbon Bond Cleavage.CHEMINFORM, Issue 19 2010Jun Terao Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a "Full Text" option. The original article is trackable via the "References" option. [source] ChemInform Abstract: Lewis Acid Promoted Carbon,Carbon Bond Cleavage of ,-Silyloxy-,-hydroxy-,-diazoesters.CHEMINFORM, Issue 32 2008Cristian Draghici Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a "Full Text" option. The original article is trackable via the "References" option. [source] ChemInform Abstract: Nucleophilic Substitution Accompanying Carbon,Carbon Bond Cleavage Assisted by a Nitro Group.CHEMINFORM, Issue 15 2008Yumi Nakaike Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a "Full Text" option. The original article is trackable via the "References" option. [source] Formation of Indene Derivatives from Bis(cyclopentadienyl)titanacyclopentadienes with Alkyl Group Migration via Carbon,Carbon Bond Cleavage.CHEMINFORM, Issue 17 2006Tamotsu Takahashi Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 200 leading journals. To access a ChemInform Abstract, please click on HTML or PDF. [source] Carbon,Carbon Bond Cleavage of Diynes Through the Hydroamination with Transition Metal Catalysts.CHEMINFORM, Issue 40 2003Tomohiro Shimada No abstract is available for this article. [source] Functional characterization of an orphan cupin protein from Burkholderia xenovorans reveals a mononuclear nonheme Fe2+ -dependent oxygenase that cleaves ,-diketonesFEBS JOURNAL, Issue 20 2009Stefan Leitgeb Cupins constitute a large and widespread superfamily of ,-barrel proteins in which a mononuclear metal site is both a conserved feature of the structure and a source of functional diversity. Metal-binding residues are contributed from two core motifs that provide the signature for the superfamily. On the basis of conservation of this two-motif structure, we have identified an ORF in the genome of Burkholderia xenovorans that encodes a novel cupin protein (Bxe_A2876) of unknown function. Recombinant Bxe_A2876, as isolated from Escherichia coli cell extract, was a homotetramer in solution, and showed mixed fractional occupancy of its 16.1 kDa subunit with metal ligands (0.06 copper; 0.11 iron; 0.17 zinc). Our quest for possible catalytic functions of Bxe_A2876 focused on Cu2+ and Fe2+ oxygenase activities known from related cupin enzymes. Fe2+ elicited enzymatic catalysis of O2 -dependent conversion of various ,-diketone substrates via a nucleophilic mechanism of carbon,carbon bond cleavage. Data from X-ray absorption spectroscopy (XAS) support a five-coordinate or six-coordinate Fe2+ center where the metal is bound by three imidazole nitrogen atoms at 1.98 Å. Results of structure modeling studies suggest that His60, His62 and His102 are the coordinating residues. In the ,best-fit' model, one or two oxygens from water and a carboxylate oxygen (presumably from Glu96) are further ligands of Fe2+ at estimated distances of 2.04 Å and 2.08 Å, respectively. The three-histidine Fe2+ site of Bxe_A2876 is compared to the mononuclear nonheme Fe2+ centers of the structurally related cysteine dioxygenase and acireductone dioxygenase, which also use a facial triad of histidines for binding of their metal cofactor but promote entirely different substrate transformations. [source] Identification of catalytically important residues in the active site of Escherichia coli transaldolaseFEBS JOURNAL, Issue 8 2001Ulrich Schörken The roles of invariant residues at the active site of transaldolase B from Escherichia coli have been probed by site-directed mutagenesis. The mutant enzymes D17A, N35A, E96A, T156A, and S176A were purified from a talB -deficient host and analyzed with respect to their 3D structure and kinetic behavior. X-ray analysis showed that side chain replacement did not induce unanticipated structural changes in the mutant enzymes. Three mutations, N35A, E96A, and T156A resulted mainly in an effect on apparent kcat, with little changes in apparent Km values for the substrates. Residues N35 and T156 are involved in the positioning of a catalytic water molecule at the active site and the side chain of E96 participates in concert with this water molecule in proton transfer during catalysis. Substitution of Ser176 by alanine resulted in a mutant enzyme with 2.5% residual activity. The apparent Km value for the donor substrate, fructose 6-phosphate, was increased nearly fivefold while the apparent Km value for the acceptor substrate, erythrose 4-phosphate remained unchanged, consistent with a function for S176 in the binding of the C1 hydroxyl group of the donor substrate. The mutant D17A showed a 300-fold decrease in kcat, and a fivefold increase in the apparent Km value for the acceptor substrate erythrose 4-phosphate, suggesting a role of this residue in carbon,carbon bond cleavage and stabilization of the carbanion/enamine intermediate. [source] | ||||||||||