Bibliografias temáticas / Reductive dehydroxylation

Literatura científica selecionada sobre o tema "Reductive dehydroxylation"

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Publicado: 20 de julho de 2024

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Artigos de revistas sobre o assunto "Reductive dehydroxylation"

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Gräwert, Tobias, Ingrid Span, Adelbert Bacher e Michael Groll. "Reductive Dehydroxylation of Allyl Alcohols by IspH Protein". Angewandte Chemie International Edition 49, n.º 47 (4 de outubro de 2010): 8802–9. http://dx.doi.org/10.1002/anie.201000833.

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Mostinski, Yelena, David Lankri, Yana Konovalov, Riva Nataf e Dmitry Tsvelikhovsky. "Proline-promoted dehydroxylation of α-ketols". Chemical Science 10, n.º 40 (2019): 9345–50. http://dx.doi.org/10.1039/c9sc02543j.

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A new single-step proline-potassium acetate promoted reductive dehydroxylation of α-ketols is reported. We introduce the unexplored reactivity of proline and, for the first time, reveal its ability to function as a reducing agent.
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Abdel-Azeim, Safwat, Abdesslem Jedidi, Jorg Eppinger e Luigi Cavallo. "Mechanistic insights into the reductive dehydroxylation pathway for the biosynthesis of isoprenoids promoted by the IspH enzyme". Chemical Science 6, n.º 10 (2015): 5643–51. http://dx.doi.org/10.1039/c5sc01693b.

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Kim, Sunggak, Li Chan e Jazreel Lim. "Iron-Catalyzed Reductive Dehydroxylation of Benzylic Alcohols Using Polymethylhydrosiloxane (PMHS)". Synlett 2011, n.º 19 (9 de novembro de 2011): 2862–66. http://dx.doi.org/10.1055/s-0031-1289857.

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Graewert, Tobias, Ingrid Span, Adelbert Bacher e Michael Groll. "ChemInform Abstract: Reductive Dehydroxylation of Allyl Alcohols by IspH Protein". ChemInform 42, n.º 6 (13 de janeiro de 2011): no. http://dx.doi.org/10.1002/chin.201106274.

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Boll, Matthias, e Georg Fuchs. "Unusual reactions involved in anaerobic metabolism of phenolic compounds". Biological Chemistry 386, n.º 10 (1 de outubro de 2005): 989–97. http://dx.doi.org/10.1515/bc.2005.115.

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AbstractAerobic bacteria use molecular oxygen as a common co-substrate for key enzymes of aromatic metabolism. In contrast, in anaerobes all oxygen-dependent reactions are replaced by a set of alternative enzymatic processes. The anaerobic degradation of phenol to a non-aromatic product involves enzymatic processes that are uniquely found in the aromatic metabolism of anaerobic bacteria: (i) ATP-dependent phenol carboxylation to 4-hydroxybenzoate via a phenylphosphate intermediate (biological Kolbe-Schmitt carboxylation); (ii) reductive dehydroxylation of 4-hydroxybenzoyl-CoA to benzoyl-CoA; and (iii) ATP-dependent reductive dearomatization of the key intermediate benzoyl-CoA in a ‘Birch-like’ reduction mechanism. This review summarizes the results of recent mechanistic studies of the enzymes involved in these three key reactions.
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Szewzyk, Ulrich, Regine Szewzyk e Bernhard Schink. "Methanogenic degradation of hydroquinone and catechol via reductive dehydroxylation to phenol". FEMS Microbiology Letters 31, n.º 2 (abril de 1985): 79–87. http://dx.doi.org/10.1111/j.1574-6968.1985.tb01134.x.

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Zhang, Jie, Hong-Kui Zhang e Pei-Qiang Huang. "Towards stereochemical control: A short formal enantioselective total synthesis of pumiliotoxins 251D and 237A". Beilstein Journal of Organic Chemistry 9 (5 de novembro de 2013): 2358–66. http://dx.doi.org/10.3762/bjoc.9.271.

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A concise enantioselective synthesis of the advanced intermediate 5 for the synthesis of pumiliotoxins (Gallagher’s intermediate) is described. The synthesis started from the regio- and trans-diastereoselective (dr = 98:2) reductive 3-butenylation of (R)-3-(tert-butyldimethylsilyloxy)glutarimide 14. After O-desilylation and Dess–Martin oxidation, the resulting keto-lactam 10 was subjected to a highly trans-stereoselective addition of the methylmagnesium iodide to give carbinol 11 as sole diastereomer. An efficient ring closure procedure consisting of ozonolysis and reductive dehydroxylation provided the indolizidine derivative 5, which completed the formal enantioselective total synthesis of pumiliotoxins 251D and 237A.
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Chan, Li Yan, Jazreel Seh Kai Lim e Sunggak Kim. "ChemInform Abstract: Iron-Catalyzed Reductive Dehydroxylation of Benzylic Alcohols Using Polymethylhydrosiloxane (PMHS)." ChemInform 43, n.º 15 (15 de março de 2012): no. http://dx.doi.org/10.1002/chin.201215029.

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Boll, Matthias, Bernhard Schink, Albrecht Messerschmidt e Peter M. H. Kroneck. "Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism". Biological Chemistry 386, n.º 10 (1 de outubro de 2005): 999–1006. http://dx.doi.org/10.1515/bc.2005.116.

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Abstract The molybdenum enzymes 4-hydroxybenzoyl-CoA reductase and pyrogallol-phloroglucinol transhydroxylase and the tungsten enzyme acetylene hydratase catalyze reductive dehydroxylation reactions, i.e., transhydroxylation between phenolic residues and the addition of water to a triple bond. Such activities are unusual for this class of enzymes, which carry either a mononuclear Mo or W center. Crystallization and subsequent structural analysis by high-resolution X-ray crystallography has helped to resolve the reaction centers of these enzymes to a degree that allows us to understand the interaction of the enzyme and the respective substrate(s) in detail, and to develop a concept for the respective reaction mechanism, at least in two cases.
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Teses / dissertações sobre o assunto "Reductive dehydroxylation"

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Jobelius, Hannah. "Etude de la métalloenzyme IspH, une cible pour le développement de nouveaux agents antibactériens". Electronic Thesis or Diss., Strasbourg, 2024. http://www.theses.fr/2024STRAF004.

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IspH est la dernière enzyme de la voie du méthylérythritol phosphate qui produit les deux précurseurs nécessaires à la biosynthèse de tous les isoprénoïdes. Cette métalloenzyme est essentielle à la survie de nombreux microorganismes dont des bactéries pathogènes et le parasite responsable du paludisme. Etant absente chez l’humain, IspH est une cible de choix pour le développement de nouveaux agents antimicrobiens. En utilisant une approche pluridisciplinaire combinant biologie moléculaire, enzymologie, spectroscopies Raman, Mössbauer et cristallographie, l’objectif de cette thèse était d’étudier le mécanisme d’IspH et plus particulièrement les paramètres qui gouvernent la formation des deux produits dans un ratio défini. Plusieurs mutants d’IspH d’E coli ont été produits, étudiés et caractérisés, et les résultats ont mis en évidence des acides aminés importants pour l’activité enzymatique et aussi pour maintenir le ratio des deux produits. Lors des études biophysiques, ces mutants ont révélé des différences au niveau de leur cofacteur, un centre [4Fe4S]2+, et de leur façon de lier le substrat par rapport à l’enzyme de type sauvage. IspH a pour la première fois été étudiée par spectroscopie Raman et une analyse détaillée a été menée
IspH is the last enzyme of the methylerythritol phosphate pathway which produces the two precursors needed for the biosynthesis of all isoprenoids. This metalloenzyme is essential for the survival of many microorganisms, among them pathogenic bacteria and the parasite responsible for malaria. Being absent in humans, IspH is a suitable target for the development of novel antimicrobial agents. Using a multidisciplinary approach combining molecular biology, enzymology, Raman and Mössbauer spectroscopy, and crystallography, the objective of this thesis was to understand the mechanism of IspH and especially the formation of the two products in a defined ratio. Several mutants were produced, studied and characterized, and the results shed light on some amino acids which are important for the enzyme activity and for maintaining the ratio of the two products. During biophysical studies, these mutants revealed differences in their cofactor, a [4Fe4S]2+ cluster, and in their way to bind the substrate as compared to the wild type enzyme. IspH has for the first time been studied using Raman spectroscopy and a detailed analysis was conducted
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Qian, Jiang. "Studies of Sulfur Reduction of Taurine and Taurine-Conjugated Bile Acids by Bile acid 7α-Dehydroxylating Bacteria". TopSCHOLAR®, 2000. http://digitalcommons.wku.edu/theses/694.

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Bile acids are C24 steroids that are derived in the liver from cholesterol and secreted into the intestinal lumen to aid in emulsification of dietary lipids and lipid-soluble vitamins. The indigenous intestinal microflora modify bile acids, producing up to 20 unique bile acid metabolites. The 7α-dehydroxylation of the bile acids is the most physiologically important bile acid biotransformation. All known intestinal bacteria capable of bile acid 7α-dehydroxylation are anaerobic, gram-positive rods of the genera Clostridium and Eubcicterium. Bile acid 7α-dehydroxylating bacteria often contain bile salt hydrolase, which hydrolyzes the peptide bond in taurine-conjugated bile acids to yield a free bile acid and taurine. Taurine is an organosulfonate containing a sulfite moiety. There have been no published reports indicating whether 7α-dehydroxylating bacteria can utilize taurine. Given that taurine and taurine-conjugated bile acids are found at great concentrations in the intestine, the ability to utilize the compound would confer a competitive advantage to these bacteria. In this study, the ability of 7α-dehydroxylating bacteria to dissimilate taurine and taurine-conjugated bile acids produce hydrogen sulfide was investigated. First, hydrogen sulfide produced by bile acid 7α-dehydroxylating bacteria cultured in tryptic soy broth and semi-defined media from taurine and taurine-conjugated bile acids was qualitatively detected by inclusion of ferric ammonium citrate in the media. The results obtained from trials utilizing anaerobic tryptic soy broth and from semi-defined medium were not consistent, suggesting that qualitative determination of sulfide by inclusion of ferric ammonium citrate is inconclusive. Then hydrogen sulfide produced by bile acid 7α-dehydroxylating bacteria cultured in modified semi-defined medium (not containing a reducing agent) over time in the presence or absence of taurine-conjugated bile acids was quantified using the methylene blue method. Sulfide concentrations in medium cultured with two different strains of bile acid 7α-dehydroxylating bacteria, Eubcicterium sp. 12708 and Clostridium sp. HD-17, in presence of 100 |j.M or 5 mM sulfonates were not significantly higher than those in the absence of sulfonate. In addition, the highest sulfide concentration determined from medium cultured with two different strains of bile acid 7α-dehydroxylating bacteria for a period of five days was not above backgroud level. These data demonstrated that these two bile acid 7α-dehydroxylating bacteria, Eubcicterium sp. 12708 and Clostridium sp. HD-17, are not capable of desulfonating taurine and taurineconjugated bile acids to produce hydrogen sulfide under the conditions tested.
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Capítulos de livros sobre o assunto "Reductive dehydroxylation"

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Iyoda, M. "1,4-Dehalogenation, Reductive Dehydroxylation, and Retro-Diels–Alder Reaction". In Monocyclic Arenes, Quasiarenes, and Annulenes, 1. Georg Thieme Verlag KG, 2010. http://dx.doi.org/10.1055/sos-sd-045-00495.

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