Search results for "substitution"

showing 10 items of 536 documents

Studies on the mechanism of PMN activation. I. By dextran sulfates.

1982

Evidence is presented that enhanced reduction of the dye nitroblue-tetrazolium (NBT) by polymorphonuclear leukocytes (PMN) which are stimulated by dextran sulfates (DS) is not exclusively due to the phagocytosis of particles formed by NBT and DS. Not only the size of phagocytizable particles but the degree of substitution determines the acceleration of NBT-reduction. A likely cause of this acceleration is the triggering of the alternative pathway of the complement activation.

ChemistryNeutrophilsPhagocytosisNitroblue TetrazoliumComplement Pathway Alternativechemical and pharmacologic phenomenaDextransHematologyGeneral MedicineComplement systemchemistry.chemical_compoundDegree of substitutionDextranBiochemistryPhagocytosisAlternative complement pathwayBiophysicsHumansBlut
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Studies of the synthesis of heterocyclic compounds. Part VII. The preparation of some new 3- and 5-amino-pyrazoles by endocyclicN-substitution of 3(5…

1982

By reaction of some 4-carbethoxy(or cyano)-3(5)-R-5(3)-aminopyrazoles 1 with 2-nitrobenzoyl chloride or 2-nitrobenzenesulfonyl chloride, a number of novel 3- and 5-amino-1-(2-nitrobenzoyl or 2-nitrobenzene-sulfonyl)pyrazoles 6 and 7 were obtained. Every compound appearing during the endocyclic N-substitution process can be identified and determined by glc. The use of nmr offers a rapid, unambigous method for determining the proposed structures.

ChemistryOrganic ChemistrySubstitution (logic)medicineCombinatorial chemistryChloridemedicine.drugJournal of Heterocyclic Chemistry
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Book Review: Electrophilic Aromatic Substitution. By R. Taylor

1991

ChemistryOrganic chemistryGeneral MedicineGeneral ChemistryElectrophilic aromatic substitutionCatalysisAngewandte Chemie International Edition in English
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Donor-acceptor substituted polyenes : orientation in mono- and multilayers

1992

Large molecules containing different chemical units whose interactions within the molecule result in new macroscopically observable effects, have become increasingly important.The organization of molecules of this type in ordered structures leads to functional molecular materials.Their use in molecular electronics requires that the units exhibit specific electronic properties. Recently, we reported on the intramolecular energy transfer through terminally substituted conjugated polyenes. An intramolecular electron transfer within donor-acceptor substituted polyenes can be achieved by introducing suitable terminal groups.

ChemistryPolyene SubstitutionsreaktionMechanical EngineeringMolecular electronicsNonlinear opticsConjugated systemPolyene540Orientation (vector space)Electron transferchemistry.chemical_compoundCrystallographyMechanics of MaterialsComputational chemistryIntramolecular forceMoleculeGeneral Materials Science
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Organometallic nucleophiles. Mechanism of halide displacement at saturated carbon by 2-pyridyl and 4-Pyridyl complexes [M(dmtc)(C5H4N-Cn)(L)] (M  Pd…

1992

Abstract A mechanistic study is reported of nucleophilic halide substitution by pyridyl complexes [M(dmtc)C 5 H 4 N- C 2 )(L)] (M  Pd or Pt; L  PMe 3 , PEt 3 or PPh 3 ) and [Pd(dmtc)C 5 H 4 N- C 4 )(L)] (L  PMe 3 or PPh 3 ) on organic halides XCH 2 R (X  Cl or Br; R  CHCH 2 , COMe, Ph, or CN) in various solvents, yielding the pyridylium derivatives [M(dmtc)1-CH 2 R)C 5 H 4 N- C 2 (L)] + and [Pd(dmtc)(1-CH 2 R)(C 5 H 4 N- C 4 (L)] + , respectively. The kinetics obey a second-order rate law: rate  k 2 [XCH 2 R][Complex]. A similar rate law is observed for the analogous reactions involving 4-dimethyl-aminopyridine (4-dmapy) as the nucleophile. The effects of solvent and leaving group, a…

ChemistryStereochemistryOrganic ChemistrySubstituentLeaving groupHalideBiochemistryMedicinal chemistryInorganic Chemistrychemistry.chemical_compoundReaction rate constantNucleophilePyridineMaterials ChemistryNucleophilic substitutionPhysical and Theoretical ChemistrySolvent effectsJournal of Organometallic Chemistry
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High Yield SNAr on 8-Halogenophenyl-BODIPY with Cyclic and Acyclic Polyamines

2014

Selective nucleophilic aromatic substitutions with several polyamines were performed in very good yields on halogeno-phenyl BODIPY derivatives containing an activating nitro group.

ChemistryStereochemistryOrganic Chemistrymacromolecular substancesFluorescenceMedicinal chemistrychemistry.chemical_compoundNucleophileNucleophilic aromatic substitutionYield (chemistry)Nucleophilic substitutionNitroPhysical and Theoretical ChemistryBODIPYEuropean Journal of Organic Chemistry
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Oligo(phenylenvinylene) mit terminaler Donor-Acceptor-Substitution

2002

ChemistryStereochemistrySubstitution (logic)General MedicineDonor acceptorAngewandte Chemie
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Determination of relative chlorophyll binding affinities in the major light-harvesting chlorophyll a/b complex.

2002

The major light-harvesting complex (LHCIIb) of photosystem II can be reconstituted in vitro from its recombinant apoprotein in the presence of a mixture of carotenoids and chlorophylls a and b. By varying the chlorophyll a/b ratio in the reconstitution mixture, the relative amounts of chlorophyll a and chlorophyll b bound to LHCIIb can be changed. We have analyzed the chlorophyll stoichiometry in recombinant wild type and mutant LHCIIb reconstituted at different chlorophyll a/b ratios in order to assess relative affinities of the chlorophyll-binding sites. This approach reveals five sites that exclusively bind chlorophyll b. Another site exhibits a slight preference of chlorophyll b over ch…

Chlorophyll bChlorophyllChlorophyll aPhotosystem IIPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiologyBiochemistrychemistry.chemical_compoundChlorophyll bindingBinding siteMolecular BiologyCarotenoidchemistry.chemical_classificationBinding SitesPeasPhotosystem II Protein ComplexCell BiologyRecombinant ProteinsB vitaminsKineticsBiochemistrychemistryAmino Acid SubstitutionChlorophyllMutagenesis Site-DirectedThe Journal of biological chemistry
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Exchange of Pigment-Binding Amino Acids in Light-Harvesting Chlorophyll a/b Protein

1999

Four amino acids in the major light-harvesting chlorophyll (Chl) a/b complex (LHCII) that are thought to coordinate Chl molecules have been exchanged with amino acids that presumably cannot bind Chl. Amino acids H68, Q131, Q197, and H212 are positioned in helixes B, C, A, and D, respectively, and, according to the LHCII crystal structure [Kühlbrandt, W., et al. (1994) Nature 367, 614-621], coordinate the Chl molecules named a(5), b(6), a(3), and b(3). Moreover, a double mutant was analyzed carrying exchanges at positions E65 and H68, presumably affecting Chls a(4) and a(5). All mutant proteins could be reconstituted in vitro with pigments, although the thermal stability of the resulting mut…

ChlorophyllChloroplastsMacromolecular SubstancesStereochemistryMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsPigment bindingLight-Harvesting Protein ComplexesTrimerBiochemistrychemistry.chemical_compoundAmino Acid SequenceAmino AcidsPeptide sequencePlant Proteinschemistry.chemical_classificationBinding SitesChlorophyll APeasPhotosystem II Protein Complexfood and beveragesAmino acidChloroplastB vitaminsAmino Acid SubstitutionchemistryChlorophyllThylakoidMutagenesis Site-DirectedCarrier ProteinsBiochemistry
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The Folding State of the Lumenal Loop Determines the Thermal Stability of Light-Harvesting Chlorophyll a/b Protein

2004

The major light-harvesting protein of photosystem II (LHCIIb) is the most abundant chlorophyll-binding protein in the thylakoid membrane. It contains three membrane-spanning alpha helices; the first and third one closely interact with each other to form a super helix, and all three helices bind most of the pigment cofactors. The protein loop domains connecting the alpha helices also play an important role in stabilizing the LHCIIb structure. Single amino acid exchanges in either loop were found to be sufficient to significantly destabilize the complex assembled in vitro [Heinemann, B., and Paulsen, H. (1999) Biochemistry 38, 14088-14093. Mick, V., Eggert, K., Heinemann, B., Geister, S., and…

ChlorophyllProtein DenaturationProtein FoldingPhotosystem IILight-Harvesting Protein ComplexesBiochemistryProtein structureTrypsinPlant Proteinschemistry.chemical_classificationChemistryChlorophyll AHydrolysisPeasTemperaturePhotosystem II Protein ComplexSodium Dodecyl SulfateProtein Structure TertiaryAmino acidKineticsCrystallographyAmino Acid SubstitutionMembrane proteinThylakoidHelixBiophysicsElectrophoresis Polyacrylamide GelProtein foldingAlpha helixBiochemistry
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