Catalase-like activity of a water-soluble complex of Ru(II)

Choua, Sylvie; Pacheco, Patricia; Coquelet, C.; Bienvenue, E.

doi:10.1016/s0162-0134(96)00091-8

Cited by 14 publications

(12 citation statements)

References 42 publications

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“…It is important to note that this compound presents lower tumor cytotoxic activity when compared with other organic ruthenium(III) compounds [33][34][35][36][37][38][39][40][41][42][43][44][45], but higher cytotoxicity than NAMI-A and derivatives [25,28,36]. Results from previous experiments [44] in which mice transplanted with sarcoma 180 cells were treated with the same ruthenium(III) complex at different time intervals and concentrations revealed that cis-[RuCl2(NH3)4]Cl is remarkably well tolerated in therapeutic doses with little or no toxicity in the host.…”

Section: Discussionmentioning

confidence: 99%

“…This suggests that similar to NAMI-A, ruthenium(III) compound binds preferentially to proteins at low concentration [20] and binds also to nucleobases only at high concentrations [22,24]. Some ruthenium compounds effectively diminish ROI levels by both catalyzing the autoxidation of glutathione [42] and displaying catalase-like activity [43]. Therefore, it is reasonable to infer that cis-(dichloro)tetraamineruthenium(III) chloride at low concentration may protect against DNA damage in Jurkat cells while inducing DNA damage at high concentration, as shown here.…”

Section: Discussionmentioning

confidence: 99%

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The Ruthenium Complex cis-(Dichloro)tetraammineruthenium(III) Chloride Presents Selective Cytotoxicity Against Murine B Cell Lymphoma (A-20), Murine Ascitic Sarcoma 180 (S-180), Human Breast Adenocarcinoma (SK-BR-3), and Human T Cell Leukemia (Jurkat) Tumor Cell Lines

Silveira-Lacerda

Vilanova-Costa

Hamaguchi

et al. 2009

Biol Trace Elem Res

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The aim of present study was to verify the in vitro antitumor activity of a ruthenium complex, cis-(dichloro)tetraammineruthenium(III) chloride (cis-[RuCl(2)(NH(3))(4)]Cl) toward different tumor cell lines. The antitumor studies showed that ruthenium(III) complex presents a relevant cytotoxic activity against murine B cell lymphoma (A-20), murine ascitic sarcoma 180 (S-180), human breast adenocarcinoma (SK-BR-3), and human T cell leukemia (Jurkat) cell lines and a very low cytotoxicity toward human peripheral blood mononuclear cells. The ruthenium(III) complex decreased the fraction of tumor cells in G0/G1 and/or G2-M phases, indicating that this compound may act on resting/early entering G0/G1 cells and/or precycling G2-M cells. The cytotoxic activity of a high concentration (2 mg mL(-1)) of cis-[RuCl(2)(NH(3))(4)]Cl toward Jurkat cells correlated with an increased number of annexin V-positive cells and also the presence of DNA fragmentation, suggesting that this compound induces apoptosis in tumor cells. The development of new antineoplastic medications demands adequate knowledge in order to avoid inefficient or toxic treatments. Thus, a mechanistic understanding of how metal complexes achieve their activities is crucial to their clinical success and to the rational design of new compounds with improved potency.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The Ruthenium Complex cis-(Dichloro)tetraammineruthenium(III) Chloride Presents Selective Cytotoxicity Against Murine B Cell Lymphoma (A-20), Murine Ascitic Sarcoma 180 (S-180), Human Breast Adenocarcinoma (SK-BR-3), and Human T Cell Leukemia (Jurkat) Tumor Cell Lines

Silveira-Lacerda

Vilanova-Costa

Hamaguchi

et al. 2009

Biol Trace Elem Res

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“…A water-soluble Ru(II) complex of a macrocycle with tertiary amines was found to be very efficient in the catalytic dismutation of hydrogen peroxide. 175 The initial rate of hydrogen peroxide decomposition by this ruthenium complex was 6x 10" 4 M _1 s _ '.…”

Section: Models Based On Soluble Complexesmentioning

confidence: 89%

Models of Heme Peroxidases and Catalases

Meunier¹

2000

Biomimetic Oxidations Catalyzed by Transition Metal Complexes

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“…Superoxide dismutases (SODs), catalase-peroxidases (KatGs) and catalases are specialized oxidoreductase enzymes for the degradation of reactive oxygen species (ROS), e.g., hydrogen peroxide, hydroxyl and superoxide radicals to avoid their accumulation and prevent the oxidative damage of cellular components, that may lead to a number of diseases such as cancer, Alzheimer’s diseases and aging [1,2,3,4]. For example, the hydroxyl and/or hydroperoxyl radicals may cause lipid peroxidation, membrane damage, DNA oxidation and cell death [5,6]. As a fine coupling of SODs and catalases, the former enzymes catalyze the dismutation of superoxide into dioxygen (1-electon oxidation) and H 2 O 2 , whilst the latter enzymes eliminate the H 2 O 2 via its decomposition by disproportionation into O 2 (2-electron oxidation) and H 2 O, resulting in the optimal intracellular concentration of a H 2 O 2 molecule [7,8,9], which acts as a second messenger in signal-transduction pathways.…”

Section: Introductionmentioning

confidence: 99%

Stability and Catalase-Like Activity of a Mononuclear Non-Heme Oxoiron(IV) Complex in Aqueous Solution

et al. 2019

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Heme-type catalase is a class of oxidoreductase enzymes responsible for the biological defense against oxidative damage of cellular components caused by hydrogen peroxide, where metal-oxo species are proposed as reactive intermediates. To get more insight into the mechanism of this curious reaction a non-heme structural and functional model was carried out by the use of a mononuclear complex [FeII(N4Py*)(CH3CN)](CF3SO3)2 (N4Py* = N,N-bis(2-pyridylmethyl)- 1,2-di(2-pyridyl)ethylamine) as a catalyst, where the possible reactive intermediates, high-valent FeIV=O and FeIII–OOH are known and spectroscopically well characterized. The kinetics of the dismutation of H2O2 into O2 and H2O was investigated in buffered water, where the reactivity of the catalyst was markedly influenced by the pH, and it revealed Michaelis–Menten behavior with KM = 1.39 M, kcat = 33 s−1 and k2(kcat/KM) = 23.9 M−1s−1 at pH 9.5. A mononuclear [(N4Py)FeIV=O]2+ as a possible intermediate was also prepared, and the pH dependence of its stability and reactivity in aqueous solution against H2O2 was also investigated. Based on detailed kinetic, and mechanistic studies (pH dependence, solvent isotope effect (SIE) of 6.2 and the saturation kinetics for the initial rates versus the H2O2 concentration with KM = 18 mM) lead to the conclusion that the rate-determining step in these reactions above involves hydrogen-atom transfer between the iron-bound substrate and the Fe(IV)-oxo species.

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Catalase-like activity of a water-soluble complex of Ru(II)

Cited by 14 publications

References 42 publications

The Ruthenium Complex cis-(Dichloro)tetraammineruthenium(III) Chloride Presents Selective Cytotoxicity Against Murine B Cell Lymphoma (A-20), Murine Ascitic Sarcoma 180 (S-180), Human Breast Adenocarcinoma (SK-BR-3), and Human T Cell Leukemia (Jurkat) Tumor Cell Lines

The Ruthenium Complex cis-(Dichloro)tetraammineruthenium(III) Chloride Presents Selective Cytotoxicity Against Murine B Cell Lymphoma (A-20), Murine Ascitic Sarcoma 180 (S-180), Human Breast Adenocarcinoma (SK-BR-3), and Human T Cell Leukemia (Jurkat) Tumor Cell Lines

Models of Heme Peroxidases and Catalases

Stability and Catalase-Like Activity of a Mononuclear Non-Heme Oxoiron(IV) Complex in Aqueous Solution

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