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Manganese Ions (manganese + ion)

Distribution by Scientific Domains

Medical Sciences	41%
Chemistry	35%

Selected Abstracts

Manganese-enhanced magnetic resonance imaging (MEMRI)

NMR IN BIOMEDICINE, Issue 8 2004
Alan P. Koretsky
Abstract Manganese ion (Mn2+) is an essential metal that participates as a cofactor in a number of critical biological functions, such as electron transport, detoxification of free radicals and synthesis of neurotransmitters. Mn2+ can enter excitable cells using some of the same transport systems as Ca2+ and it can bind to a number of intracellular sites because it has high affinity for Ca2+ and Mg2+ binding sites on proteins and nucleic acids. Paramagnetic forms of manganese ions are potent MRI relaxation agents. Indeed, Mn2+ was the first contrast agent proposed for use in MRI. Recently, there has been renewed interest in combining the strong MRI relaxation effects of Mn2+ with its unique biology, in order to further expand the already broad assortment of useful information that can be measured by MRI. Such an approach has been continuously developed in the past several years to provide unique tissue contrast, to assess tissue viability, to act as a surrogate marker of calcium influx into cells and to trace neuronal connections. This special issue of NMR in Biomedicine on manganese-enhanced MRI (MEMRI) is aimed at providing the readers of this journal with an extensive review of some of the most prominent applications of MEMRI in biological systems. Written by several of the leaders in the field, the reviews and original research articles featured in this special issue are likely to offer an exciting and inspiring view of the broad range of applications of MEMRI. Copyright © 2004 John Wiley & Sons, Ltd. [source]

Ion channel activity of transmembrane segment 6 of Escherichia coli proton-dependent manganese transporter

BIOPOLYMERS, Issue 8 2010
uková
Abstract Synthetic peptides corresponding to the sixth transmembrane segment (TMS6) of secondary-active transporter MntH (Proton-dependent Manganese Transporter) from Escherichia coli and its two mutations in the functionally important conserved histidine residue were used as a model for structure,function study of MntH. The secondary structure of the peptides was estimated in different environments using circular dichroism spectroscopy. These peptides interacted with and adopted helical conformations in lipid membranes. Electrophysiological experiments demonstrated that TMS6 was able to form multi-state ion channels in model biological membranes. Electrophysiological properties of these weakly cation-selective ion channels were strongly dependent on the surrounding pH. Manganese ion, as a physiological substrate of MntH, enhanced the conductivity of TMS6 channels, influenced the transition between closed and open states, and affected the peptide conformations. Moreover, functional properties of peptides carrying two different mutations of His211 were analogous to in vivo functional characteristics of Nramp/MntH proteins mutated at homologous residues. Hence, a single functionally important TMS can retain some of the functional properties of the full-length protein. These findings could contribute to understanding the structure,function relationship at the molecular level. However it remains unclear to what extent the peptide-specific channel activity represents a functional aspect of the full-length membrane carrier protein. © 2010 Wiley Periodicals, Inc. Biopolymers 93: 718,726, 2010. This article was originally published online as an accepted preprint. The "Published Online" date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com [source]

Manganese ions as intracellular contrast agents: proton relaxation and calcium interactions in rat myocardium

NMR IN BIOMEDICINE, Issue 2 2003
Wibeke Nordhøy
Abstract Paramagnetic manganese (Mn) ions (Mn2+) are taken up into cardiomyocytes where they are retained for hours. Mn content and relaxation parameters, T1 and T2, were measured in right plus left ventricular myocardium excised from isolated perfused rat hearts. In the experiments 5,min wash-in of MnCl2 were followed by 15,min wash-out to remove extracellular (ec) Mn2+ MnCl2, 25 and 100,µM, elevated tissue Mn content to six and 12 times the level of control (0,µM MnCl2). Variations in perfusate calcium (Ca2+) during wash-in of MnCl2 and experiments including nifedipine showed that myocardial slow Ca2+ channels are the main pathway for Mn2+ uptake and that Mn2+ acts as a pure Ca2+ competitor and a preferred substrate for slow Ca2+ channel entry. Inversion recovery analysis at 20,MHz revealed two components for longitudinal relaxation: a short T1,,,1 and a longer T1,,,2. Approximate values for control and Mn-treated hearts were in the range 600,125,ms for T1,,,1 and 2200,750,ms for T1,,,2. The population fractions were about 59 and 41% for the short and the long component, respectively. The intracellular (ic) R1,,,1 and R2,,,1 correlated best with tissue Mn content. Applying two-site exchange analyses on the obtained T1 data yielded results in parallel to, but also differing from, results reported with an ec contrast agent. The calculated lifetime of ic water (,ic) of about 10,s is compatible with a slow water exchange in the present excised cardiac tissue. The longitudinal relaxivity of Mn ions in ic water [60 (s mM),1] was about one order of magnitude higher than that of MnCl2 in water in vitro [6.9 (s mM),1], indicating that ic Mn-protein binding is an important potentiating factor in relaxation enhancement. Copyright © 2003 John Wiley & Sons, Ltd. [source]

Structure of spinach acetohydroxyacid isomeroreductase complexed with its reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-ribose

ACTA CRYSTALLOGRAPHICA SECTION D, Issue 4 2000
Karine Thomazeau
Acetohydroxyacid isomeroreductase catalyses a two-step reaction composed of an alkyl migration followed by an NADPH-dependent reduction. Both steps require a divalent cation and the first step has a strong preference for magnesium. Manganese ions are highly unfavourable to the reaction: only 3% residual activity is observed in the presence of this cation. Acetohydroxyacid isomeroreductase has been crystallized with its substrate, 2-aceto-2-hydroxybutyrate (AHB), Mn2+ and NADPH. The 1.6,Å resolution electron-density map showed the reaction product (2,3-dihydroxy-3-methylvalerate, DHMV) and a density corresponding to (phospho)-ADP-ribose instead of the whole NADP+. This is one of the few structures of an enzyme complexed with its reaction product. The structure of this complex was refined to an R factor of 19.3% and an Rfree of 22.5%. The overall structure of the enzyme is very similar to that of the complex with the reaction-intermediate analogue IpOHA [N -hydroxy- N -isopropyloxamate; Biou et al. (1997), EMBO J.16, 3405,3415]. However, the active site shows some differences: the nicotinamide is cleaved and the surrounding amino acids have rearranged accordingly. Comparison between the structures corresponding to the reaction intermediate and to the end of the reaction allowed the proposal of a reaction scheme. Taking this result into account, the enzyme was crystallized with Ni2+ and Zn2+, for which only 0.02% residual activity were measured; however, the crystals of AHB/Zn/NADPH and of AHB/Ni/NADPH also contain the reaction product. Moreover, mass-spectrometry measurements confirmed the cleavage of nicotinamide. [source]

Chemical and Electrochemical Behaviours of a New Phenolato-Bridged Complex [(L)MnIIMnII(L)]2+.

EUROPEAN JOURNAL OF INORGANIC CHEMISTRY, Issue 21 2006
Dinuclear Mono-µ-Oxido [(L)MnIII(µ-O)MnIII/IV(L)]2+/3+ Species, Pathways to Mononuclear Chlorido [(L)MnII/III/IVCl]0/1/2+
Abstract The X-ray structure of a new dinuclear phenolato-bridged Mn2II complex abbreviated as [(L)MnMn(L)]2+ (1), where LH is the [N4O] phenol containing ligand N,N -bis(2-pyridylmethyl)- N, -salicylidene-ethane-1,2-diamine ligand, is reported. A J value of ,3.3 cm,1 (H = ,J,1·,2) was determined from the magnetic measurements and the 9.4 GHz EPR spectra of both powder and frozen acetonitrile solution samples were analyzed with temperature. The cyclic voltammetry of 1 displays a reversible anodic wave at E1/2 = 0.46 V vs. SCE associated with the two-electron oxidation of 1 yielding the dinuclear Mn2III complex [(L)MnMn(L)]4+ (2). The easy air oxidation of 1 gives the mono-,-oxido Mn2III complex [(L)Mn(, - O)Mn(L)]2+ (3). A rational route to the formation of the mixed-valence Mn2III,IV complex [(L)Mn(, - O)Mn(L)]3+ (4) starting from 1 by bulk electrolysis at EP = 0.75 V vs. SCE in the presence of one equiv. of base per manganese ion is also briefly reported. Addition of chloride ions to 1 led to the cleavage of the phenolato bridges to give the mononuclear MnII complex [(L)MnCl] (5). Cyclic voltammetry of 5 displays two reversible anodic waves at E1/2 = 0.21 and E1/2 = 1.15 V vs. SCE, assigned to the two successive one-electron abstractions giving the MnIII and MnIV species [(L)MnCl]+ (6) and [(L)MnCl]2+ (7), respectively. The electronic signatures from UV/Visible and EPR spectroscopy of the electrochemically prepared samples of 6 and 7 confirmed the respective oxidation states. For instance, 7 displays a broad and intense absorption band characteristic of a phenolato to MnIV charge-transfer transition at 690 nm (2000 M,1,cm,1) and its 9.4 GHz EPR spectrum shows a strong transition at g = 5.2 consistent with a rhombically distorted S = 3/2 system with a zero-field splitting dominating the Zeeman effect. (© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2006) [source]

Asymmetric epoxidation of chromenes catalyzed by chiral pyrrolidine SalenMn(III) complexes with an anchored functional group

APPLIED ORGANOMETALLIC CHEMISTRY, Issue 10 2008
Xiang Zhang
Abstract Chiral pyrrolidine SalenMn(III) complexes with an anchored functional group at the Naza -substituent in the pyrrolidine backbone were synthesized, and used as catalysts for asymmetric epoxidation of substituted chromenes. The complex 1 with an anchored imidazole as acceptor could effectively catalyze epoxidation of substituted chromenes in the absence of expensive additive 4-phenyl pyridine N -oxide (PPNO) by the coordination of the anchored organic base to the central manganese ion. Complexes 2 and 3 with a quaternary ammonium salt unit at the Naza -substituent in the pyrrolidine backbone displayed higher activities than Jacobsen catalyst and the analogous complex 4 without anchored functional group in the aforementioned reaction. Copyright © 2008 John Wiley & Sons, Ltd. [source]

A Feasible Enzymatic Process for d -Tagatose Production by an Immobilized Thermostable l -Arabinose Isomerase in a Packed-Bed Bioreactor

BIOTECHNOLOGY PROGRESS, Issue 2 2003
Hye-Jung Kim
To develop a feasible enzymatic process for d -tagatose production, a thermostable l -arabinose isomerase, Gali152, was immobilized in alginate, and the galactose isomerization reaction conditions were optimized. The pH and temperature for the maximal galactose isomerization reaction were pH 8.0 and 65 °C in the immobilized enzyme system and pH 7.5 and 60 °C in the free enzyme system. The presence of manganese ion enhanced galactose isomerization to tagatose in both the free and immobilized enzyme systems. The immobilized enzyme was more stable than the free enzyme at the same pH and temperature. Under stable conditions of pH 8.0 and 60 °C, the immobilized enzyme produced 58 g/L of tagatose from 100 g/L galactose in 90 h by batch reaction, whereas the free enzyme produced 37 g/L tagatose due to its lower stability. A packed-bed bioreactor with immobilized Gali152 in alginate beads produced 50 g/L tagatose from 100 g/L galactose in 168 h, with a productivity of 13.3 (g of tagatose)/(L-reactor·h) in continuous mode. The bioreactor produced 230 g/L tagatose from 500 g/L galactose in continuous recycling mode, with a productivity of 9.6 g/(L·h) and a conversion yield of 46%. [source]

Effects of ouabain on contractions induced by manganese ions in Ca2+ -free, isotonic solutions with varying concentrations of K+ in guinea-pig taenia coli

FUNDAMENTAL & CLINICAL PHARMACOLOGY, Issue 3 2005
Tetsuyuki Nasu
Abstract The action of ouabain, a cell membrane Na+, K+ -ATPase blocker, on contractions induced by manganese ions (Mn2+) in Ca2+ -free, isotonic solutions with varying concentrations of K+ in the external medium were investigated in order to evaluate the underlying role of external Na+ in Mn2+ -induced contractions in isolated taenia coli of the guinea-pig. Mn2+ at 5 mm induced greater contractions as external isotonic K+ concentrations progressively increased from 10 to 100 mm. Ouabain (2 × 10,4 m) completely inhibited tension development stimulated by 5 mm Mn2+ in isotonic, 30 mm K+ (96 mm Na+) medium. Whereas, the tension inhibitory effects of ouabain became progressively weaker as isotonic, external K+ concentrations increased to 60 mm, which successively decreased external Na+ concentrations. Eventually, ouabain failed to affect contractions stimulated by Mn2+ in isotonic, 126 mm K+, Na+ -deficient medium. Ouabain caused progressively greater increase in cellular Na+ concentrations as the Na+ concentrations increased in the isotonic, K+ medium. While, pyruvate, which penetrates cell independently of external Na+, reversed the inhibition of tension by ouabain in isotonic, 30 mm K+, Na+ -sufficient (96 mm) medium containing 5 mm Mn2+. These results suggested that Mn2+ induced the contraction, which was maintained by glucose transport depending on external Na+, in the case of Na+ -sufficient medium in K+ -depolarized taenia coli. However, it induced the contraction independent of external Na+, in the case of Na+ -deficient, K+ medium. Ouabain might exhibit greater inhibition of the contraction induced by Mn2+ as the decrease in the Na+ gradient across the cell membranes continues. [source]

Magnetic and Structural Investigation of ZnSe Semiconductor Nanoparticles Doped With Isolated and Core-Concentrated Mn2+ Ions

ADVANCED FUNCTIONAL MATERIALS, Issue 15 2009
Christina Graf
X-Ray magnetic circular dichroism (XMCD) experiments on diluted magnetic semiconductor nanocrystals (2,7,nm) are reported in order to study their local electronic structure and magnetic properties. ZnSe nanoparticles containing either single manganese ions (Mn2+) distributed in the lattice of the entire particle or a MnSe core in the center are prepared using high temperature approaches. The Mn2+ concentration is varied between less than one to several tens of manganese ions per nanocrystal. For all samples it is shown that the Mn2+ is exclusively present in the bulk of ZnSe nanoparticles with no evidence for oxidation to higher Mn-oxidation states. The magnetic ions are highly polarized inside the nanocrystals reaching about 80% of the theoretical value of a pure d5 state under identical conditions for the case of isolated manganese ions. Nanocrystals with a MnSe core ZnSe shell structure reach <50% of this value. Thus, their polarization is significantly more hindered, which is due to the significantly enhanced Mn,Mn interactions and a more distorted crystalline lattice. In contrast, no coupling between the manganese centers is observed in the nanoparticles doped samples with low concentrations of Mn2+, indicating that these ions are isolated in the bulk of the nanoparticles. [source]

Formation and decay of the ABTS derived radical cation: A comparison of different preparation procedures

INTERNATIONAL JOURNAL OF CHEMICAL KINETICS, Issue 12 2002
Carola Henriquez
Bleaching of a preformed solution of the blue-green radical cation 2,2,-azinobis (3-ethylbenzothizoline-6-sulfonic acid) (ABTS+·) has been extensively used to evaluate the antioxidant capacity of complex mixtures and individual compounds. The reaction of the preformed radical with free-radical scavengers can be easily monitored by following the decay of the sample absorbance at 734 nm. The ABTS radical cation can be prepared employing different oxidants. Results obtained using MnO2 as oxidant show that the presence of manganese ions increases the rate of [ABTS]+· autobleaching in a concentration-dependent manner. The radicals can also be obtained by oxidizing ABTS with 2,2, -azobis(2-amidinopropane)hydrochloride (AAPH) or peroxodisulfate (PDS). The oxidation by AAPH takes place with a large activation energy and a low reaction order in ABTS. The data support a mechanism in which the homolysis of AAPH is the rate-limiting step, followed by the reaction of ABTS with the peroxyl radicals produced after the azocompound thermolysis. On the other hand, the low activation energy measured employing PDS, as well as the kinetic law, are compatible with the occurrence of a bimolecular reaction between the oxidant and ABTS. Regarding the use of ABTS-based methodologies for the evaluation of free radical scavengers, radical cations obtained employing AAPH as oxidant can be used only at low temperatures, conditions where further decomposition of the remaining AAPH is minimized. The best results are obtained with ABTS derived radicals generated in the reaction of PDS with an ABTS/PDS concentration ratio equal (or higher) to two. However, even with radicals prepared by this procedure, stoichiometric coefficients considerably larger than two are obtained for the consumption of the radical cation employing tryptophane or p -terbutylphenol as reductants. This casts doubts on the use of ABTS-based procedures for the estimation of antioxidant capacities. © 2002 Wiley Periodicals, Inc. Int J Chem Kinet 34: 659,665, 2002 [source]

Delayed changes in T1 -weighted signal intensity in a rat model of 15-minute transient focal ischemia studied by magnetic resonance imaging/spectroscopy and synchrotron radiation X-ray fluorescence

MAGNETIC RESONANCE IN MEDICINE, Issue 3 2006
Xuxia Wang
Abstract Previous studies have found that rats subjected to 15-min transient middle cerebral artery occlusion (MCAO) show neurodegeneration in the dorsolateral striatum only, and the resulting striatal lesion is associated with increased T1 -weighted (T1W) signal intensity (SI) and decreased T2 -weighted (T2W) SI at 2,8 weeks after the initial ischemia. It has been shown that the delayed increase in T1W SI in the ischemic region is associated with deposition of paramagnetic manganese ions. However, it has been suggested that other mechanisms, such as tissue calcification and lipid accumulation, also contribute to the relaxation time changes. To clarify this issue, we measured changes in relaxation times, lipid accumulation, and elemental distributions in the brain of rats subjected to 15-min MCAO using MRI, in vivo 1H MR spectroscopy (MRS), and synchrotron radiation X-ray fluorescence (SRXRF). The results show that a delayed (2 weeks after ischemia) increase in T1W SI in the ischemic striatum is associated with significant increases in manganese, calcium, and iron, but without evident accumulation of MRS-visible lipids or hydroxyapatite precipitation. It was also found that 15-min MCAO results in acutely reduced N-acetylaspartate (NAA)/creatine (Cr) ratio in the ipsilateral striatum, which recovers to the control level at 2 weeks after ischemia. Magn Reson Med, 2006. © 2006 Wiley-Liss, Inc. [source]

Detection of the anoxic depolarization of focal ischemia using manganese-enhanced MRI

MAGNETIC RESONANCE IN MEDICINE, Issue 1 2003
Ichio Aoki
Abstract Mismatch between diffusion- and perfusion-weighted MRI was used to indicate a treatable area following focal ischemia, called the penumbra. Activity-induced manganese contrast MRI has been reported as a new visualization method for neural activation using manganese ions as a depolarization-dependent contrast agent. It is well known that energy failure induced by cerebral ischemia produces anoxic depolarization. The purpose of this study was to detect manganese accumulation caused by permanent middle cerebral artery occlusion (MCAO) of rat brain and to compare regional differences between manganese accumulation and decreased apparent diffusion coefficient (ADC). The ratios of signal intensity of manganese-enhanced MRI in the ipsilateral cortex to that in the contralateral cortex were 171.0 ± 17.5% in MCAO group and 108.4 ± 13.2% in the sham group. In addition, the enhanced region was much smaller than the area which was detected as having a reduced ADC. Magn Reson Med 50:7,12, 2003. © 2003 Wiley-Liss, Inc. [source]

Manganese-enhanced magnetic resonance imaging (MEMRI)

Synthesis of MnGeO3 polycrystalline and single-crystal samples and comparative analysis of their magnetic properties

PHYSICA STATUS SOLIDI (B) BASIC SOLID STATE PHYSICS, Issue 1 2009
N. V. Sapronova
Abstract MnGeO3 single crystals have been grown by a flux method. The obtained MnGeO3 is orthorhombic; a Pbca space group does not undergo any structural phase transitions in the range from room temperature to 900 °C. Magnetic measurements carried out for the first time on the MnGeO3 single crystal have revealed higher values (TN = 38 K and , = ,100 K) as compared to the data for polycrystalline samples reported in the literature (TN = 10 K and 14 K, , = ,54 K and ,46 K). These magnetic parameters for polycrystalline samples synthesized by us are close to the literature data. A Mössbauer spectrum taken at T = 300 K for a sample containing 5% Fe257O3 shows that manganese ions, Mn2+, occupy two nonequivalent positions and iron is included in a sublattice as Fe2+ and distributed among two positions substituting Mn2+. In this study, the magnetic characteristics are shown to be sensitive even to minor impurity amounts. The MnGeO3 magnetic structure and one of possible reasons causing the effect of impurities on the MnGeO3 magnetic properties are considered in the framework of a simple indirect coupling model. (© 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim) [source]

Interaction of an echinomycin,DNA complex with manganese ions

ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 7 2009
Roland Pfoh
The crystal structure of an echinomycin,d(ACGTACGT) duplex interacting with manganese(II) was solved by Mn-SAD using in-house data and refined to 1.1,Å resolution against synchrotron data. This complex crystallizes in a different space group compared with related complexes and shows a different mode of base pairing next to the bis-intercalation site, suggesting that the energy difference between Hoogsteen and Watson,Crick pairing is rather small. The binding of manganese to N7 of guanine is only possible because of DNA unwinding induced by the echinomycin, which might help to explain the mode of action of the drug. [source]