Building, characterising and catalytic activity testing of Co–C-protected amino acid complexes covalently grafted onto chloropropylated silica gel

Varga, Gábor; Tímár, Zoltán; Csendes, Zita; Bajnóczi, Éva G.; Carlson, Stefan; Canton, Sophie E.; Bagi, L.; Sipos, Pál; Pálinkó, István

doi:10.1016/j.molstruc.2014.11.039

Cited by 3 publications

(1 citation statement)

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“…Sulfur-containing organic compounds—especially cysteine and its derivatives—as bioactive ingredients or functional bioconjugates have been widely applied in chemo-enzymatic syntheses as well as composing biomedicines for many years [ 1 , 2 , 3 ]. Numerous previous studies demonstrated considerable improvement in the biocatalytic activity of living and artificial enzymes containing thiol- and/or disulfide-containing redox moieties [ 4 , 5 , 6 ]. Additionally, biomimetic compounds modelled after natural enzymes including cystine side chains proved to be efficient biosensors and serodiagnostic test molecules as well as catalysts in fermentation applications [ 7 , 8 , 9 , 10 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

Oxidation of Cysteinate Anions Immobilized in the Interlamellar Space of CaAl-Layered Double Hydroxide

et al. 2021

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L-Cysteinate-intercalated CaAl-layered double hydroxide (LDH) was prepared by the co-precipitation method producing highly crystalline hydrocalumite phase with a well-pillared interlayer gallery. The obtained materials were characterized by X-ray diffractometry, IR as well as Raman spectroscopies. By performing interlamellar oxidation reactions with peracetic acid as oxidant, oxidation of cysteinate to cystinate in aqueous and cysteinate sulfenic acid in acetonic suspensions occurred. The oxidations could be performed under mild conditions, at room temperature, under neutral pH and in air. It has been shown that the transformation pathways are due to the presence of the layered structure, that is, the confined space of the LDH behaved as molecular reactor.

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