(Benzene­carbothio­amide-κS)­penta­carbonyl­tungsten(0)

The asymmetric unit of the title complex, [W(C7H7NS)(CO)5], comprises two independent mol­ecules. In each, the W atom is coordinated by five CO groups and the S atom of the benzencarbothioamide ligand in a distorted octa­hedral geometry. The crystal packing can be described as undulating layers of W(CO)5 and benzene­carbothio­amide parallel to (001). In the crystal, components are linked via inter­molecular N—H⋯O and C—H⋯O hydrogen bonds to form a dimeric chains along the [010] direction. Intra­molecular N—H⋯C inter­actions are also observed

Penta­carbon­yl(imidazolidine-2-thione-κS)tungsten(0)

In the title complex, [W(C3H6N2S)(CO)5], the W atom displays an octa­hedral coordination with five CO mol­ecules and an imidazolidine-2-thione mol­ecule. The W(CO)5 unit is coordinated by the cyclic thione ligand through a W—S dative bond. The W—S and C—S bond lengths are 2.599 (2) and 1.711 (9) Å, respectively. This last distance is significantly longer than that of free cyclic thio­ureas. The geometry of the title compound suggests sp 3-hybridization of the S atom caused by the greatly polarized linkage W—S—C bond angle, which is close to tetra­hedral [109.50 (3)°]. In the crystal packing, N—H⋯O and N—H⋯S hydrogen-bonding inter­actions stabilize the structure and build up chains parallel to [101]

Enterococcus faecalis utilizes maltose by connecting two incompatible metabolic routes via a novel maltose-6-P phosphatase (MapP)

Similar to Bacillus subtilis, Enterococcus faecalis transports and phosphorylates maltose via a phosphoenolpyruvate (PEP):maltose phosphotransferase system (PTS). The maltose-specific PTS permease is encoded by the malT gene. However, E. faecalis lacks a malA gene encoding a 6-phospho-a-glucosidase, which in B. subtilis hydrolyses maltose 6-P into glucose and glucose 6-P. Instead, an operon encoding a maltose phosphorylase (MalP), a phosphoglucomutase and a mutarotase starts upstream from malT. MalP was suggested to split maltose 6-P into glucose 1-P and glucose 6-P. However, purified MalP phosphorolyses maltose but not maltose 6-P. We discovered that the gene downstream from malT encodes a novel enzyme (MapP) that dephosphorylates maltose 6-P formed by the PTS. The resulting intracellular maltose is cleaved by MalP into glucose and glucose 1-P. Slow uptake of maltose probably via a maltodextrin ABC transporter allows poor growth for the mapP but not the malP mutant. Synthesis of MapP in a B. subtilis mutant accumulating maltose 6-P restored growth on maltose. MapP catalyses the dephosphorylation of intracellular maltose 6-P, and the resulting maltose is converted by the B. subtilis maltose phosphorylase into glucose and glucose 1-P. MapP therefore connects PTS-mediated maltose uptake to maltose phosphorylase-catalysed metabolism. Dephosphorylation assays with a wide variety of phosphosubstrates revealed that MapP preferably dephosphorylates disaccharides containing an O-aglycosyl linkageFil: Mokhtari, Abdelhamid. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Francia. University Mentouri. Faculty of Natural Science and Life. Department of Biochemistry-Microbiology. Laboratory of Environmental Biology; ArgeliaFil: Blancato, Victor Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Repizo, Guillermo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Henry, Céline. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; FranciaFil: Pikis, Andreas. Center for Drug Evaluation and Research. Food and Drug Administration; Estados UnidosFil: Bourand, Alexa. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; FranciaFil: Alvarez, Maria de Fatima. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Immel, Stefan. Technische Universität Darmstad. Institut für Organische Chemie; AlemaniaFil: Mechakra Maza, Aicha. University Mentouri. Faculty of Natural Science and Life. Department of Biochemistry-Microbiology. Laboratory of Environmental Biology; ArgeliaFil: Hartke, Axel. Universite de Caen Basse Normandie; FranciaFil: Thompson, John. National Institutes of Health. Laboratory of Cell and Developmental Biology. Microbial Biochemistry and Genetics Section; Estados UnidosFil: Magni, Christian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Deutscher, Josef. Institut National de la Recherche Agronomique. Microbiologie de l’Alimentation au Service de la Santé Humaine; Franci

Marquage de 2-aminothiazole avec une unité cyclohéxadiène fer tricabonyle. Etude structurale et activité antibactérienne du complexe marqué (1-4-η-5-N-2-aminothiazoliocyclohexa-1,3-diène) fer tricarbonyle.

La réaction de 2-aminothiazole C3H4N2S avec le complexe tétrafluoroborate (1-4-η-5-N-pyridiniocyclohexa-1,3-diène) fer tricarbonyle [C11H12NFe(CO)3]+[BF4]-1, précurseur du cation marqueur [ (1-5-η-C6H7) Fe(CO)3]+ donne un nouveau complexe (1-4-η-5-N-2-aminothiazolocyclohexa-1,3-diène) fer tricarbonyle de formule C9H10N2S Fe(CO)3 2. La structure de ce complexe a été caractérisée par les méthodes spectroscopiques (IR, RMN 1H) suivie d’une étude structurale par diffraction des RX qui a montré que le complexe marqué 2 adopte un énantiomère exo. Dans l’édifice cristallin, les composants de la structure sont liés par des liaisons hydrogènes intermoléculaires de type N-H…N formant des chaînes dimériques le long de l’axe b. L’activité antimicrobienne du ligand libre 2-aminothiazole a montré une activité antibactérienne importante. Après sa complexation par le marqueur organo fer tricarbonyle, cette activité a augmenté. The reaction of 2-aminothiazole C3H4N2S with tricarbonyl (1- 4-η-5-N-pyridiniocyclohexa-1,3-diene) iron tetrafluoroborate complex [C11H12NFe(CO)3]+[BF4]- 1, a precursor of the highly reactive cation [Fe(CO)3(1-5-η-C6H7)]+, afforded a new tricarbonyl (1-4-η-5-N-2-aminothiazoliocyclohexa-1,3-diene) iron complex of formula C9H10N2S Fe(CO)3 2. The structure of this complex was characterized by IR, 1H NMR spectroscopy and single crystal X-ray diffraction analysis which showed that the labelled complex 2 adopts an exo-enantiomer. In the crystal packing, the components of the structure are linked via intermolecular N-H…N hydrogen bonds to form a dimeric chains running along the b-axis direction. The antimicrobial activity of the free ligands 2-aminothiazole showed an important antibacterial activity .After labeling them, this activity has increased for the complex 2.The accepted manuscript in pdf format is listed with the files at the bottom of this page. The presentation of the authors' names and (or) special characters in the title of the manuscript may differ slightly between what is listed on this page and what is listed in the pdf file of the accepted manuscript; that in the pdf file of the accepted manuscript is what was submitted by the author

Neocapture: regulatory competition in an open market world

This paper shows that inter-regulatory competition can have powerful pro-consumer effects in an open economy world even when the consumers have little political influence. These findings overturn the welfare implications of capture theories that show that regulators do not vigorously pursue public interests. The paper also points to the kinds of markets where the political competition has more or less powerful effects (fixed cost technology case). Since markets have become more integrated over time, there are obvious implications for the evolution of regulation.globalization, regulatory competition, regulatory collusion, capture theory, economic theory of regulation, game theory,

Transport and catabolism of pentitols by Listeria monocytogenes

Transposon insertion into Listeria monocytogenes Imo2665, which encodes an EIIC of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), was found to prevent D-arabitol utilization. We confirm this result with a deletion mutant and show that Lmo2665 is also required for D-xylitol utilization. We therefore called this protein EIICAxl. Both pentitols are probably catabolized via the pentose phosphate pathway (PPP) because Imo2665 belongs to an operon, which encodes the three PTSAxl components, two sugar-P dehydrogenases, and most PPP enzymes. The two dehydrogenases oxidize the pentitol-phosphates produced during PTS-catalyzed transport to the PPP intermediate xylulose-5-P. L. monocytogenes contains another PTS, which exhibits significant sequence identity to PTSAxl. Its genes are also part of an operon encoding PPP enzymes. Deletion of the EIIC-encoding gene (Imo0508) affected neither D-arabitol nor D-xylitol utilization, although D-arabitol induces the expression of this operon. Both operons are controlled by MtIR/LicR-type transcription activators (Lmo2668 and Lnno0501, respectively). Phosphorylation of Lmo0501 by the soluble PTSAxl components probably explains why D-arabitol also induces the second pentitol operon. Listerial virulence genes are submitted to strong repression by PTS sugars, such as glucose. However, D-arabitol inhibited virulence gene expression only at high concentrations, probably owing to its less efficient utilization compared to glucose

Transport and catabolism of pentitols by Listeria monocytogenes

Transposon insertion into Listeria monocytogenes Imo2665, which encodes an EIIC of the phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS), was found to prevent D-arabitol utilization. We confirm this result with a deletion mutant and show that Lmo2665 is also required for D-xylitol utilization. We therefore called this protein EIICAxl. Both pentitols are probably catabolized via the pentose phosphate pathway (PPP) because Imo2665 belongs to an operon, which encodes the three PTSAxl components, two sugar-P dehydrogenases, and most PPP enzymes. The two dehydrogenases oxidize the pentitol-phosphates produced during PTS-catalyzed transport to the PPP intermediate xylulose-5-P. L. monocytogenes contains another PTS, which exhibits significant sequence identity to PTSAxl. Its genes are also part of an operon encoding PPP enzymes. Deletion of the EIIC-encoding gene (Imo0508) affected neither D-arabitol nor D-xylitol utilization, although D-arabitol induces the expression of this operon. Both operons are controlled by MtIR/LicR-type transcription activators (Lmo2668 and Lnno0501, respectively). Phosphorylation of Lmo0501 by the soluble PTSAxl components probably explains why D-arabitol also induces the second pentitol operon. Listerial virulence genes are submitted to strong repression by PTS sugars, such as glucose. However, D-arabitol inhibited virulence gene expression only at high concentrations, probably owing to its less efficient utilization compared to glucose

The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions

The bacterial phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system (PTS) carries out both catalytic and regulatory functions. It catalyzes the transport and phosphorylation of a variety of sugars and sugar derivatives but also carries out numerous regulatory functions related to carbon, nitrogen, and phosphate metabolism, to chemotaxis, to potassium transport, and to the virulence of certain pathogens. For these different regulatory processes, the signal is provided by the phosphorylation state of the PTS components, which varies according to the availability of PTS substrates and the metabolic state of the cell. PEP acts as phosphoryl donor for enzyme I (EI), which, together with HPr and one of several EIIA and EIIB pairs, forms a phosphorylation cascade which allows phosphorylation of the cognate carbohydrate bound to the membrane-spanning EIIC. HPr of firmicutes and numerous proteobacteria is also phosphorylated in an ATP-dependent reaction catalyzed by the bifunctional HPr kinase/phosphorylase. PTS-mediated regulatory mechanisms are based either on direct phosphorylation of the target protein or on phosphorylation-dependent interactions. For regulation by PTS-mediated phosphorylation, the target proteins either acquired a PTS domain by fusing it to their N or C termini or integrated a specific, conserved PTS regulation domain (PRD) or, alternatively, developed their own specific sites for PTS-mediated phosphorylation. Protein-protein interactions can occur with either phosphorylated or unphosphorylated PTS components and can either stimulate or inhibit the function of the target proteins. This large variety of signal transduction mechanisms allows the PTS to regulate numerous proteins and to form a vast regulatory network responding to the phosphorylation state of various PTS components