36507-30-9Relevant articles and documents
Detection and characterization of an oxomanganese(V) porphyrin complex by rapid-mixing stopped-flow spectrophotometry
Groves, John T.,Lee, Jinbo,Marla, Sudhakar S.
, p. 6269 - 6273 (1997)
The first detection and characterization of oxomanganese(V) porphyrin complexes under ambient catalytic conditions is described. The reaction of (tetra-(N-methylpyridyl)porphyrinato)manganese(III) [Mn(III)TMPyP] with a variety of oxidants such as m-chloroperoxybenzoic acid (m-CPBA), HSO5-, and ClO- has been shown to produce the same, short-lived intermediate (1) by stopped-flow spectrophotometry. The Soret maximum of 1 was found at 443 nm, intermediate between that of oxomanganese(IV) (428 nm) and Mn(III)TMPyP (462 nm), thus facilitating its detection. The rate of formation of 1 from Mn(III)TMPyP followed second-order kinetics, first order in Mn(III) porphyrin and first order in oxidant. The rate constants have the following order: m- CPBA (2.7 x 107 M1 S1)> HSO5- 6.9 x 105 M1 s1 ? CIO (6.3 x 105 M1 s-1). Once formed, the intermediate species 1 was rapidly converted to oxoMn(IV) (2) by one-electron reduction with a first-order rate constant of 5.7 s-1. The oxoMn(IV) species 2 was relatively stable under the reaction conditions, decaying slowly to Mn(III)TMPyP with a first-order rate constant of 0.027 s-1. The identity of 1 as an oxomanganese(V) complex was indicated by its reactivity. The one-electron reduction of I to oxoMn(IV) was greatly accelerated by nitrite ion (k = 1.5 x 107 M-1 s-1). However, the reaction between nitrite and oxoMn(IV) is much slower (k = 1.4 x 102 M-1 s-1). The oxoMn(V) intermediate 1 was shown to be highly reactive toward olefins, affording epoxide products. By contrast, oxoMn(IV) (2) was not capable of effecting the same reaction under these conditions. In the presence of carbamazepine (3) efficient oxygen transfer from the highly reactive oxoMn(V) (1) to the olefin (second-order rate constant of 6.5 x 105 M-1 s-1) resulted in the conversion of I directly back to Mn(III)TMPyP without the appearance of the stable oxoMn(IV) intermediate 2. With m-CPBA as the oxidant in the presence of H218O, the product epoxide was shown to contain 35% 18O, consistent with an O-exchange-labile oxoMn(V) intermediate. Nitrite ion inhibited the epoxidation reaction competitively by one electron reduction of the oxoMn(V) intermediate to the unreactive oxoMn(IV).
Carbamazepine oxidation catalyzed by manganese porphyrins: Effects of the β-bromination of the macrocycle and the choice of oxidant
Carvalhoda-Silva, Dayse,Mac Leod, Tatiana Cristina Oliveira,De Faria, André Luiz,Dos Santos, Joicy Santamalvina,De Carvalho, Maria Eliza Moreira Dai,Rebouas, Júlio Santos,Idemori, Ynara Marina,Assis, Marilda Das Dores
, p. 25 - 30 (2011)
Carbamazepine (CBZ), which is one of the most commonly prescribed antiepileptic drugs and also used in the treatment of trigeminal neuralgia and psychiatric disorders, is metabolized primarily by the cytochromes P450. A homologous series of β-brominated porphyrins derived from 5,10,15,20-tetrakis(4-carbomethoxyphenyl)porphyrinatomanganese(III) chloride, i.e., Mn(III)(BrxTCMPP)Cl (x = 0, 2, 4, 6, and 8), was investigated as cytochrome P450 models for CBZ oxidation in CH2Cl2 by iodosylbenzene, iodobenzene diacetate, tert-butyl hydroperoxide, meta-chloroperoxybenzoic acid, and hydrogen peroxide. Unlike previous studies on metalloporphyrin-based CBZ oxidation, which yielded CBZ epoxide (CBZ-EP) as the sole product, the Mn(III)(BrxTCMPP)Cl systems catalyzed both the oxidation of CBZ to CBZ-EP and the formation of the respective vicinal diol, CBZ-DiOH. The influence of β-bromination of the macrocycle and the choice of the oxidant on the catalytic properties of the Mn(III)(BrxTCMPP)Cl (x = 0, 2, 4, 6, and 8) series were examined. Some partially β-brominated Mn-porphyrins surpass the corresponding octabrominated analogue in efficiency and selectivity, but the extent by which the β-bromination affects the catalytic activity depends on the choice of oxidant. The selectivity for CBZ oxidation to yield the respective epoxide reached 100% or ～94% by using tert-butyl hydroperoxide or hydrogen peroxide as oxygen donors, respectively.
"Redox tautomerism" in high-valent metal-oxo-aquo complexes. Origin of the oxygen atom in epoxidation reactions catalyzed by water-soluble metalloporphyrins
Bernadou, Jean,Fabiano, Anne-Sylvie,Robert, Anne,Meunier, Bernard
, p. 9375 - 9376 (1994)
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Mass spectrometric characterization of carbamazepine-10,11-epoxide, a carbamazepine metabolite isolated from human urine.
Frigerio,Fanelli,Biandrate,Passerini,Morselli,Garattini
, p. 1144 - 1147 (1972)
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Role of human arylacetamide deacetylase (aadac) on hydrolysis of eslicarbazepine acetate and effects of aadac genetic polymorphisms on hydrolase activity
Hirosawa, Keiya,Fukami, Tatsuki,Tashiro, Kiyomichi,Sakai, Yoshiyuki,Kisui, Fumiya,Nakano, Masataka,Nakajima, Miki
, p. 322 - 329 (2021/03/22)
Human arylacetamide deacetylase (AADAC) plays a role in the detoxification or activation of drugs and is sometimes involved in the incidence of toxicity by catalyzing hydrolysis reactions. AADAC prefers compounds with relatively small acyl groups, such as acetyl groups. Eslicarbazepine acetate, an antiepileptic drug, is a prodrug rapidly hydrolyzed to eslicarbazepine. We sought to clarify whether AADAC might be responsible for the hydrolysis of eslicarbazepine acetate. Eslicarbazepine acetatewas efficiently hydrolyzed by human intestinal and liver microsomes and recombinant human AADAC. The hydrolase activities in human intestinal and liver microsomes were inhibited by epigallocatechin gallate, a specific inhibitor of AADAC, by 82% and 88% of the control, respectively. The hydrolase activities in liver microsomes from 25 human livers were significantly correlated (r = 0.87, P a factor affecting the enzyme activity and drug response.
Carbamazepine derivatives with P2X4 receptor-blocking activity
Tian, Maoqun,Abdelrahman, Aliaa,Weinhausen, Stephanie,Hinz, Sonja,Weyer, Stefanie,Dosa, Stefan,El-Tayeb, Ali,Müller, Christa E.
supporting information, p. 1077 - 1088 (2014/02/14)
Antagonists for the P2 receptor subtype P2X4, an ATP-activated cation channel receptor, have potential as novel drugs for the treatment of neuropathic pain and other inflammatory diseases In the present study, a series of 47 carbamazepine derivatives including 32 novel compounds were designed, synthesized, and evaluated as P2X4 receptor antagonists Their potency to inhibit ATP-induced calcium influx in 1321N1 astrocytoma cells stably transfected with the human P2X4 receptor was determined Additionally, species selectivity (human, rat, mouse) and receptor subtype selectivity (P2X4 vs P2X1, 2, 3, 7) were investigated for selected derivatives The most potent compound of the present series, which exhibited an allosteric mechanism of P2X4 inhibition, was N,N-diisopropyl-5H-dibenz[b,f]azepine-5-carboxamide (34, IC50 of 3.44 μM) The present study extends the so far very limited knowledge on structure-activity relationships of P2X4 receptor antagonists
