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1.
J Am Chem Soc ; 143(50): 21286-21293, 2021 Dec 22.
Artículo en Inglés | MEDLINE | ID: mdl-34825564

RESUMEN

Atomic-scale reproducibility and tunability endorse magnetic molecules as candidates for spin qubits and spintronics. A major challenge is to implant those molecular spins into circuit geometries that may allow one, two, or a few spins to be addressed in a controlled way. Here, the formation of mechanically bonded, magnetic porphyrin dimeric rings around carbon nanotubes (mMINTs) is presented. The mechanical bond places the porphyrin magnetic cores in close contact with the carbon nanotube without disturbing their structures. A combination of spectroscopic techniques shows that the magnetic geometry of the dimers is preserved upon formation of the macrocycle and the mMINT. Moreover, the metallic core selection determines the spin location in the mMINT. The suitability of mMINTs as qubits is explored by measuring their quantum coherence times (Tm). Formation of the dimeric ring preserves the Tm found in the monomer, which remains in the µs scale for mMINTs. The carbon nanotube is used as vessel to place the molecules in complex circuits. This strategy can be extended to other families of magnetic molecules. The size and composition of the macrocycle can be tailored to modulate magnetic interactions between the cores and to introduce magnetic asymmetries (heterometallic dimers) for more complex molecule-based qubits.

2.
J Exp Bot ; 69(15): 3703-3714, 2018 06 27.
Artículo en Inglés | MEDLINE | ID: mdl-29701804

RESUMEN

Nitric oxide (NO) is a signaling molecule with multiple functions in plants. Given its critical importance and reactivity as a gaseous free radical, we have examined NO production in legume nodules using electron paramagnetic resonance (EPR) spectroscopy and the specific fluorescent dye 4,5-diaminofluorescein diacetate. Also, in this context, we critically assess previous and current views of NO production and detection in nodules. EPR of intact nodules revealed that nitrosyl-leghemoglobin (Lb2+NO) was absent from bean or soybean nodules regardless of nitrate supply, but accumulated in soybean nodules treated with nitrate that were defective in nitrite or nitric oxide reductases or that were exposed to ambient temperature. Consequently, bacteroids are a major source of NO, denitrification enzymes are required for NO homeostasis, and Lb2+NO is not responsible for the inhibition of nitrogen fixation by nitrate. Further, we noted that Lb2+NO is artifactually generated in nodule extracts or in intact nodules not analyzed immediately after detachment. The fluorescent probe detected NO formation in bean and soybean nodule infected cells and in soybean nodule parenchyma. The NO signal was slightly decreased by inhibitors of nitrate reductase but not by those of nitric oxide synthase, which could indicate a minor contribution of plant nitrate reductase and supports the existence of nitrate- and arginine-independent pathways for NO production. Together, our data indicate that EPR and fluorometric methods are complementary to draw reliable conclusions about NO production in plants.


Asunto(s)
Fabaceae/metabolismo , Leghemoglobina/metabolismo , Óxido Nítrico/metabolismo , Fijación del Nitrógeno , Espectroscopía de Resonancia por Spin del Electrón , Colorantes Fluorescentes , Nódulos de las Raíces de las Plantas/metabolismo , Simbiosis
3.
Photosynth Res ; 133(1-3): 273-287, 2017 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-28032235

RESUMEN

The photosynthetic cytochrome c 550 from the marine diatom Phaeodactylum tricornutum has been purified and characterized. Cytochrome c 550 is mostly obtained from the soluble cell extract in relatively large amounts. In addition, the protein appeared to be truncated in the last hydrophobic residues of the C-terminus, both in the soluble cytochrome c 550 and in the protein extracted from the membrane fraction, as deduced by mass spectrometry analysis and the comparison with the gene sequence. Interestingly, it has been described that the C-terminus of cytochrome c 550 forms a hydrophobic finger involved in the interaction with photosystem II in cyanobacteria. Cytochrome c 550 was almost absent in solubilized photosystem II complex samples, in contrast with the PsbO and Psb31 extrinsic subunits, thus suggesting a lower affinity of cytochrome c 550 for the photosystem II complex. Under iron-limiting conditions the amount of cytochrome c 550 decreases up to about 45% as compared to iron-replete cells, pointing to an iron-regulated synthesis. Oxidized cytochrome c 550 has been characterized using continuous wave EPR and pulse techniques, including HYSCORE, and the obtained results have been interpreted in terms of the electrostatic charge distribution in the surroundings of the heme centre.


Asunto(s)
Grupo Citocromo c/metabolismo , Diatomeas/metabolismo , Fotosíntesis , Secuencia de Aminoácidos , Grupo Citocromo c/química , Grupo Citocromo c/aislamiento & purificación , Espectroscopía de Resonancia por Spin del Electrón , Modelos Moleculares , Peso Molecular , Complejo de Proteína del Fotosistema II/metabolismo , Electricidad Estática
4.
Inorg Chem ; 53(23): 12384-95, 2014 Dec 01.
Artículo en Inglés | MEDLINE | ID: mdl-25285579

RESUMEN

Homoleptic organocobalt(III) compounds with formula [NBu4][Co(III)(C6X5)4] [X = F (3), Cl (4)] were obtained in reasonable yields by chemical oxidation of the corresponding divalent species [NBu4]2[Co(II)(C6X5)4] [X = F (1), Cl (2)]. The [Co(III)(C6X5)4](-)/[Co(II)(C6X5)4](2-) couples are electrochemically related by quasi-reversible, one-electron exchange processes at moderate potential: E1/2 = -0.29 (X = F) and -0.36 V (X = Cl) versus saturated calomel electrode. The [Co(III)(C6X5)4](-) anions in salts 3 and 4 show an unusual square-planar geometry as established by single-crystal X-ray diffraction methods. According to their stereochemistry, these Co(III) derivatives (d(6)) are paramagnetic non-Kramers systems with a large zero-field splitting contribution and no observable electron paramagnetic resonance (EPR) spectrum. The thermal dependence of their magnetic susceptibilities can be explained in terms of a spin-Hamiltonian formalism with S = 1 ground state (intermediate spin) and substantial spin-orbit contribution. The magnetic properties of the square-planar d(7) parent species [NBu4]2[Co(II)(C6X5)4] were also thoroughly studied both at microscopic (EPR) and macroscopic levels (alternating current and direct current magnetization measurements). They behave as S = 1/2 (low spin) systems with mainly (dz(2))(1) electron configuration and a certain degree of s-orbital admixture that has been quantified. The electronic structures of all four open-shell [Co(C6X5)4](q-) compounds (q = 1, 2) accounting for their respective magnetic properties are based on a common orbital energy-level diagram.

5.
Phys Chem Chem Phys ; 16(47): 26203-12, 2014 Dec 21.
Artículo en Inglés | MEDLINE | ID: mdl-25363087

RESUMEN

In this contribution we present the study of the thermal dependence of the ENDOR spectra of flavodoxin at low temperatures which reveals the dynamics of the methyl groups bound to the flavin moiety in flavoproteins. The methyl groups behave as quantum rotors locked by a deep rotational well and undergoing a tunneling process. At room temperature, methyl rotors are locked and the hopping motion is slow. This picture of the dynamics of the methyl groups of the flavin ring is quite different from the one usually accepted and has relevant consequences on the understanding of the mechanisms of flavoproteins.


Asunto(s)
Flavoproteínas/química , Teoría Cuántica , Temperatura
6.
Mater Horiz ; 10(11): 5214-5222, 2023 Oct 30.
Artículo en Inglés | MEDLINE | ID: mdl-37725390

RESUMEN

Molecular spins are considered as the quantum hardware to build hybrid quantum processors in which coupling to superconducting devices would provide the means to implement the necessary coherent manipulations. As an alternative to large magnetically-dilute crystals or concentrated nano-scale deposits of paramagnetic molecules that have been studied so far, the use of pre-formed sub-micronic spherical particles of a doped Gd@Y hydroxycarbonate is evaluated here. Particles with an adjustable number of spin carriers are prepared through the control of both particle size and doping. Bulk magnetic properties and continuous wave and time-domain-EPR spectroscopy show that the Gd spins in these particles are potential qubits with robust quantum coherence. Monolayers of densely-packed particles are then formed interfacially and transferred successfully to the surface of Nb superconducting resonators. Alternatively, these particles are disposed at controlled localizations as isolated groups of a few particles through Dip-Pen Nanolithography using colloidal organic dispersions as ink. Altogether, this study offers new material and methodologies relevant to the development of viable hybrid quantum processors.

7.
J Med Chem ; 66(12): 7849-7867, 2023 06 22.
Artículo en Inglés | MEDLINE | ID: mdl-37265008

RESUMEN

Photodynamic therapy holds great promise as a non-invasive anticancer tool against drug-resistant cancers. However, highly effective, non-toxic, and reliable photosensitizers with operability under hypoxic conditions remain to be developed. Herein, we took the advantageous properties of COUPY fluorophores and cyclometalated Ir(III) complexes to develop novel PDT agents based on Ir(III)-COUPY conjugates with the aim of exploring structure-activity relationships. The structural modifications carried out within the coumarin scaffold had a strong impact on the photophysical properties and cellular uptake of the conjugates. All Ir(III)-COUPY conjugates exhibited high phototoxicity under green light irradiation, which was attributed to the photogeneration of ROS, while remaining non-toxic in the dark. Among them, two hit conjugates showed excellent phototherapeutic indexes in cisplatin-resistant A2780cis cancer cells, both in normoxia and in hypoxia, suggesting that photoactive therapy approaches based on the conjugation of far-red/NIR-emitting COUPY dyes and transition metal complexes could effectively tackle in vitro acquired resistance to cisplatin.


Asunto(s)
Antineoplásicos , Fotoquimioterapia , Humanos , Cisplatino , Antineoplásicos/farmacología , Antineoplásicos/química , Fármacos Fotosensibilizantes/farmacología , Fármacos Fotosensibilizantes/uso terapéutico , Fármacos Fotosensibilizantes/química , Relación Estructura-Actividad
8.
Chem Sci ; 14(14): 3899-3906, 2023 Apr 05.
Artículo en Inglés | MEDLINE | ID: mdl-37035710

RESUMEN

A quantum spin liquid (QSL) is an elusive state of matter characterized by the absence of long-range magnetic order, even at zero temperature, and by the presence of exotic quasiparticle excitations. In spite of their relevance for quantum communication, topological quantum computation and the understanding of strongly correlated systems, like high-temperature superconductors, the unequivocal experimental identification of materials behaving as QSLs remains challenging. Here, we present a novel 2D heterometallic oxalate complex formed by high-spin Co(ii) ions alternating with diamagnetic Rh(iii) in a honeycomb lattice. This complex meets the key requirements to become a QSL: a spin ½ ground state for Co(ii), determined by spin-orbit coupling and crystal field, a magnetically-frustrated triangular lattice due to the presence of antiferromagnetic correlations, strongly suppressed direct exchange interactions and the presence of equivalent interfering superexchange paths between Co centres. A combination of electronic paramagnetic resonance, specific heat and ac magnetic susceptibility measurements in a wide range of frequencies and temperatures shows the presence of strong antiferromagnetic correlations concomitant with no signs of magnetic ordering down to 15 mK. These results show that bimetallic oxalates are appealing QSL candidates as well as versatile systems to chemically fine tune key aspects of a QSL, like magnetic frustration and superexchange path geometries.

9.
Photosynth Res ; 112(3): 193-204, 2012 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-22855209

RESUMEN

A study of the in vitro reconstitution of sugar beet cytochrome b(559) of the photosystem II is described. Both α and ß cytochrome subunits were first cloned and expressed in Escherichia coli. In vitro reconstitution of this cytochrome was carried out with partially purified recombinant subunits from inclusion bodies. Reconstitution with commercial heme of both (αα) and (ßß) homodimers and (αß) heterodimer was possible, the latter being more efficient. The absorption spectra of these reconstituted samples were similar to that of the native heterodimer cytochrome b(559) form. As shown by electron paramagnetic resonance and potentiometry, most of the reconstituted cytochrome corresponded to a low spin form with a midpoint redox potential +36 mV, similar to that from the native purified cytochrome b(559). Furthermore, during the expression of sugar beet and Synechocystis sp. PCC 6803 cytochrome b(559) subunits, part of the protein subunits were incorporated into the host bacterial inner membrane, but only in the case of the ß subunit from the cyanobacterium the formation of a cytochrome b(559)-like structure with the bacterial endogenous heme was observed. The reason for that surprising result is unknown. This in vivo formed (ßß) homodimer cytochrome b(559)-like structure showed similar absorption and electron paramagnetic resonance spectral properties as the native purified cytochrome b(559). A higher midpoint redox potential (+126 mV) was detected in the in vivo formed protein compared to the in vitro reconstituted form, most likely due to a more hydrophobic environment imposed by the lipid membrane surrounding the heme.


Asunto(s)
Citocromos b/química , Citocromos b/metabolismo , Embryophyta/fisiología , Complejo de Proteína del Fotosistema II/fisiología , Synechocystis/fisiología , Beta vulgaris/enzimología , Beta vulgaris/genética , Beta vulgaris/fisiología , Clonación Molecular , Citocromos b/genética , Espectroscopía de Resonancia por Spin del Electrón , Embryophyta/enzimología , Embryophyta/genética , Escherichia coli/enzimología , Escherichia coli/genética , Regulación Enzimológica de la Expresión Génica , Cuerpos de Inclusión , Oxidación-Reducción , Fotosíntesis , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Proteínas Recombinantes de Fusión , Synechocystis/enzimología , Synechocystis/genética , Zea mays/enzimología , Zea mays/genética , Zea mays/fisiología
10.
Chem Commun (Camb) ; 58(35): 5375-5378, 2022 Apr 28.
Artículo en Inglés | MEDLINE | ID: mdl-35411892

RESUMEN

A designed dimetallic Fe(II) helicate made with biphenylene-bridged bispyrazolylpyridine ligands and exhibiting a process of spin crossover at temperatures above ambient is shown to encapsulate an S = 5/2 tris-oxalato Fe(III) ion. The spin relaxation dynamics of this guest are strongly reduced upon encapsulation.

11.
Commun Chem ; 3(1): 176, 2020 Nov 20.
Artículo en Inglés | MEDLINE | ID: mdl-36703386

RESUMEN

Artificial magnetic molecules can host several spin qubits, which could then implement small-scale algorithms. In order to become of practical use, such molecular spin processors need to increase the available computational space and warrant universal operations. Here, we design, synthesize and fully characterize dissymetric molecular dimers hosting either one or two Gadolinium(III) ions. The strong sensitivity of Gadolinium magnetic anisotropy to its local coordination gives rise to different zero-field splittings at each metal site. As a result, the [LaGd] and [GdLu] complexes provide realizations of distinct spin qudits with eight unequally spaced levels. In the [Gd2] dimer, these properties are combined with a Gd-Gd magnetic interaction, sufficiently strong to lift all level degeneracies, yet sufficiently weak to keep all levels within an experimentally accessible energy window. The spin Hamiltonian of this dimer allows a complete set of operations to act as a 64-dimensional all-electron spin qudit, or, equivalently, as six addressable qubits. Electron paramagnetic resonance experiments show that resonant transitions between different spin states can be coherently controlled, with coherence times TM of the order of 1 µs limited by hyperfine interactions. Coordination complexes with embedded quantum functionalities are promising building blocks for quantum computation and simulation hybrid platforms.

12.
Chem Sci ; 11(38): 10337-10343, 2020 Oct 14.
Artículo en Inglés | MEDLINE | ID: mdl-36196278

RESUMEN

We show that a [Er-Ce-Er] molecular trinuclear coordination compound is a promising platform to implement the three-qubit quantum error correction code protecting against pure dephasing, the most important error in magnetic molecules. We characterize it by preparing the [Lu-Ce-Lu] and [Er-La-Er] analogues, which contain only one of the two types of qubit, and by combining magnetometry, low-temperature specific heat and electron paramagnetic resonance measurements on both the elementary constituents and the trimer. Using the resulting parameters, we demonstrate by numerical simulations that the proposed molecular device can efficiently suppress pure dephasing of the spin qubits.

13.
Front Plant Sci ; 11: 600336, 2020.
Artículo en Inglés | MEDLINE | ID: mdl-33329665

RESUMEN

In plants, symbiotic hemoglobins act as carriers and buffers of O2 in nodules, whereas nonsymbiotic hemoglobins or phytoglobins (Glbs) are ubiquitous in tissues and may perform multiple, but still poorly defined, functions related to O2 and/or nitric oxide (NO). Here, we have identified a Glb gene of the model legume Medicago truncatula with unique properties. The gene, designated MtGlb1-2, generates four alternative splice forms encoding Glbs with one or two heme domains and 215-351 amino acid residues. This is more than double the size of any hemoglobin from plants or other organisms described so far. A combination of molecular, cellular, biochemical, and biophysical methods was used to characterize these novel proteins. RNA-sequencing showed that the four splice variants are expressed in plant tissues. MtGlb1-2 is transcriptionally activated by hypoxia and its expression is further enhanced by an NO source. The gene is preferentially expressed in the meristems and vascular bundles of roots and nodules. Two of the proteins, bearing one or two hemes, were characterized using mutants in the distal histidines of the hemes. The Glbs are extremely reactive toward the physiological ligands O2, NO, and nitrite. They show very high O2 affinities, NO dioxygenase activity (in the presence of O2), and nitrite reductase (NiR) activity (in the absence of O2) compared with the hemoglobins from vertebrates and other plants. We propose that these Glbs act as either NO scavengers or NO producers depending on the O2 tension in the plant tissue, being involved in the fast and fine tuning of NO concentration in the cytosol in response to sudden changes in O2 availability.

15.
Biophys J ; 96(1): 141-52, 2009 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-18835911

RESUMEN

Oxidized cytochrome c(6) from Anabaena PCC 7119 was studied by electron spin echo envelope modulation spectroscopy. Hyperfine couplings of the unpaired electron with several nuclei were detected, in particular those of the nitrogens bound to the iron atom. Combining the experimental information here presented and previous continuous wave-electron paramagnetic resonance and electron nuclear double resonance results, some details on the electronic structure of the heme center in the protein are obtained. These results are discussed on the basis of a molecular model that considers one unpaired electron localized mainly in the iron d orbitals and propagation of the spin density within the heme center via spin polarization of the nitrogen sigma-orbitals. The coexistence of two heme forms at physiological pH values in this c-type cytochrome is also discussed taking into account the experimental evidence.


Asunto(s)
Citocromos c6/química , Algoritmos , Anabaena , Proteínas Bacterianas/química , Campos Electromagnéticos , Espectroscopía de Resonancia por Spin del Electrón/métodos , Electrones , Hemo/química , Concentración de Iones de Hidrógeno , Compuestos de Hierro/química , Modelos Químicos , Modelos Moleculares , Compuestos de Nitrógeno/química , Análisis Espectral/métodos
16.
J Photochem Photobiol B ; 152(Pt B): 308-17, 2015 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-26183783

RESUMEN

The cytochrome b559 is a heme-bridged heterodimeric protein with two subunits, α and ß. Both subunits from Synechocystis sp. PCC 6803 have previously been cloned and overexpressed in Escherichia coli and in vivo reconstitution experiments have been carried out. The formation of homodimers in the bacterial membrane with endogenous heme was only observed in the case of the ß-subunit (ß/ß) but not with the full length α-subunit. In the present work, reconstitution of a homodimer (α/α) cytochrome b559 like structure was possible using a chimeric N-terminus α-subunit truncated before the amino acid isoleucine 17, eliminating completely a short amphipathic α-helix that lays on the surface of the membrane. Overexpression and in vivo reconstitution in the bacteria was clearly demonstrated by the brownish color of the culture pellet and the use of a commercial monoclonal antibody against the fusion protein carrier, the maltoside binding protein, and polyclonal antibodies against a synthetic peptide of the α-subunit from Thermosynechococcus elongatus. Moreover, a simple partial purification after membrane solubilization with Triton X-100 confirmed that the overexpressed protein complex corresponded with the maltoside binding protein-chimeric α-subunit cytochrome b559 like structure. The features of the new structure were determined by UV-Vis, electron paramagnetic resonance and redox potentiometric techniques. Ribbon representations of all possible structures are also shown to better understand the mechanism of the cytochrome b559 maturation in the bacterial cytoplasmic membrane.


Asunto(s)
Grupo Citocromo b/química , Complejo de Proteína del Fotosistema II/química , Multimerización de Proteína , Subunidades de Proteína/química , Synechocystis/enzimología , Secuencia de Aminoácidos , Membrana Celular/metabolismo , Grupo Citocromo b/metabolismo , Maltosa/metabolismo , Modelos Moleculares , Datos de Secuencia Molecular , Complejo de Proteína del Fotosistema II/metabolismo , Estructura Cuaternaria de Proteína , Estructura Secundaria de Proteína , Subunidades de Proteína/metabolismo , Synechocystis/citología
17.
J Magn Reson ; 218: 153-62, 2012 May.
Artículo en Inglés | MEDLINE | ID: mdl-22446506

RESUMEN

A complete study of Anabaena flavodoxin in the neutral semiquinone state by means of the EPR pulse technique HYSCORE is here presented. The results provide new information about the hyperfine interactions of the unpaired electronic spin and the nuclei in the isoalloxazine ring. This allows a better knowledge of the electronic structure of the neutral flavin radical within the protein. Combination of these results with other previously obtained by using other EPR related techniques allowed producing a very precise mapping of the flavin spin distribution in the neutral semiquinone state. This information can be very useful for determining the relationship between the electronic structure and mechanisms in flavoproteins. An experimental protocol for measuring the electronic structure details available to date is suggested.


Asunto(s)
Anabaena/química , Flavinas/química , Flavodoxina/química , Anisotropía , Espectroscopía de Resonancia por Spin del Electrón , Transporte de Electrón , Flavoproteínas/química , Isomerismo , Microondas , Quinonas/química
18.
FEBS J ; 279(12): 2231-46, 2012 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-22521074

RESUMEN

The transcriptional repressor Fur (ferric uptake regulator) is one of the most important switches regulating prokaryotic iron metabolism. Cyanobacterial FurA binds heme in the micromolar concentration range and this interaction negatively affects its in vitro DNA binding ability in a concentration-dependent manner. Using site-directed mutagenesis along with difference absorption UV-visible, circular dichroism and electronic paramagnetic resonance spectroscopies, we further analyse the nature of heme binding in FurA. Our data point to Cys141, within a Cys-Pro motif, as an axial ligand of the Fe(III) high-spin heme. In the Fe(II) oxidation state, the heme shows low-spin form with an electronic absorption spectrum typical of six-coordinated low-spin heme proteins with a Soret absorption maximum blue-shifted by 25 nm in relation to typical low-spin thiolate-ligated Fe(II) heme proteins. Moreover, the ferrous C141S mutant shows Soret, α and ß bands almost identical to those observed for ferrous wild-type heme-FurA, indicating that the heme in ferrous C141S is in the same six-coordinated heme ligation as the ferrous native form. Therefore, Cys141 is not a ligand of the Fe(II) heme centre, suggesting a redox-dependent ligand switch undergone by this regulator. Our results indicate that the binding of heme to FurA exhibits the same physicochemical features as previously described for heme sensor proteins.


Asunto(s)
Anabaena/metabolismo , Proteínas Bacterianas/metabolismo , Hemo/metabolismo , Anabaena/genética , Proteínas Bacterianas/genética , Dicroismo Circular , Mutagénesis Sitio-Dirigida , Espectrofotometría Ultravioleta
20.
J Phys Chem B ; 114(46): 15345-53, 2010 Nov 25.
Artículo en Inglés | MEDLINE | ID: mdl-21028863

RESUMEN

A study of the hydrogen hyperfine couplings of the Mn-cluster of the oxygen-evolving complex of Photosystem II in the S(2) state of the Kok cycle by means of hyperfine sublevel correlation spectroscopy was achieved. Features corresponding to hyperfine interaction of at least two hydrogen nuclei were detected. Combining our results with previous ENDOR data, hyperfine constants were determined, and by using a model for the structure and electronic spin state of the Mn-cluster, relevant structural information of the S(2) state was obtained. This new information can be used for improving our knowledge about the structure and function of the Mn-cluster during light-driven water oxidation reaction in oxygenic photosynthetic organisms.


Asunto(s)
Hidrógeno/química , Manganeso/química , Complejo de Proteína del Fotosistema II/química , Análisis Espectral/métodos , Oxidación-Reducción , Fotosíntesis
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