Search results for "Enzyme model"

showing 5 items of 5 documents

A Versatile and Convenient Method for the Functionalization of Porphyrins

2001

International audience; The condensation of 3-(chloromethyl)benzoyl chloride with different atropisomers of meso-(tetra-o-aminophenyl)porphyrin (TAPP), followed by the reaction of a series of nucleophilic reagents leads, among others, to precursors of biomimetic models of heme proteins such as cytochrome c oxidase (CcO). This synthesis can also be applied as an efficient two-step reaction to obtain highly functionalized porphyrin derivatives potentially useful for cation binding.

Cation bindingAtropisomerHemeproteinPorphyrinsChemistryEnzyme modelsOrganic ChemistryPorphyrinCombinatorial chemistry[ CHIM ] Chemical SciencesHeme proteinschemistry.chemical_compoundBenzoyl chlorideNucleophileReagentCationspolycyclic compounds[CHIM]Chemical SciencesOrganic chemistrySurface modificationPhysical and Theoretical ChemistryOxidoreductases
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Front Cover: Redox‐Controlled Stabilization of an Open‐Shell Intermediate in a Bioinspired Enzyme Model (Eur. J. Inorg. Chem. 31/2018)

2018

Inorganic ChemistryFront coverChemical engineeringChemistryEnzyme modelOpen shellRedoxEuropean Journal of Inorganic Chemistry
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Redox‐Controlled Stabilization of an Open‐Shell Intermediate in a Bioinspired Enzyme Model

2018

Inorganic Chemistrychemistry010405 organic chemistryMolybdenumEnzyme modelchemistry.chemical_element010402 general chemistryPhotochemistry01 natural sciencesRedoxOpen shell0104 chemical sciencesEuropean Journal of Inorganic Chemistry
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High Turnover Catalase Activity of a Mixed‐Valence Mn II Mn III Complex with Terminal Carboxylate Donors

2015

The neutral dimanganese(II,III) complex [Mn-2(BCPMP)-(OAc)(2)] [1; BCPMP3- = 2,6-bis({(carboxymethyl)[(1-pyridyl)-methyl] amino} methyl)-4-methylphenolato] has been synthesized and characterized. The complex contains two terminal carboxylate donors. Complex 1 was found to be an effective catalyst for the disproportionation of H2O2 with high catalytic rate and a turnover number of 7500, the highest turnover reported to date for a catalase mimic. The rates and TON were significantly higher than recorded for a dicationic dimanganese( II,III) counterpart ([Mn-2(BPBP)(OAc)(2)]center dot(ClO4)(2), 2; BPBP- = 2,6-bis{[bis(2-pyridylmethyl)amino]methyl}-4-butylphen-olato), which lacks the terminal c…

ManganeseReaction mechanismbiologyChemistryEnzyme modelsReaction mechanismschemistry.chemical_elementDisproportionationManganeseCatalaseHydrogen peroxidePhotochemistryMedicinal chemistryCatalysisTurnover numberInorganic Chemistrychemistry.chemical_compoundDinucleating ligandsCatalytic cycleCatalasebiology.proteinCarboxylateta116European Journal of Inorganic Chemistry
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Chemie an starren Grenzflächen, 10. Kinetisches Verhalten einiger an „Isothiocyanato-Aerosil” immobilisierter Esterasen – Analogversuche mit Insulin

1988

Amino-Aerosil wird mit Thiophosgen nach Gl. (1) in Isothiocyanato-Aerosil 2 (NCS-Aerosil) ubergefuhrt. Trypsin, Cholinesterase und Acetylcholinesterase werden an 2 nach Gl. (2) immobilisiert. Die Aktivitat der immobilisierten Esterasen wird untersucht auf (a) Lagerstabilitat, (b) Temperaturbestandigkeit und (c) pH-Abhangigkeit. Das kinetische Verhalten der immobilisierten Enzyme wird verglichen mit dem der freien, aber mit n-Butylisothiocyanat behandelten Esterasen. Am Beispiel der Cholinesterase, die uber unterschiedliche Ankergruppen mit Aerosil verknupft wurde, wird der Einflus unterschiedlicher Spacergruppen auf die Hydrolysegeschwindigkeit studiert. Aerosile, die mit Acetylcholin-Analo…

chemistry.chemical_classificationbiologyImmobilized enzymeStereochemistryOrganic ChemistryTrypsinEsteraseAcetylcholinesteraseHydrolysischemistry.chemical_compoundEnzymechemistryEnzyme modelbiology.proteinmedicinePhysical and Theoretical ChemistryCholinesterasemedicine.drugLiebigs Annalen der Chemie
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