On the EUV Spectrum of Li I

Mannervik, S.; Cederquist, H.

doi:10.1088/0031-8949/34/2/009

Cited by 15 publications

(17 citation statements)

References 15 publications

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“…They have used this IP and the ls2s2p P'-ls2p2p P energy (33871(2)cm ' [15,18]) to determined the T of the 1s2p2p P and, thereafter, the rest of the core-excited doublets. Using [53] have also derived the transition wavelength of the Li is 21 to the core-excited doublets to high precision using the available experimental data. We will use our prediction to make a critical comparison with these results.…”

Section: Complex-rotation Calculationmentioning

confidence: 99%

Absolute term energy of core-excited doublet states of lithium

Chen

Chung

1994

Phys. Rev. A

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Thirteen core-excited lithium doublet states of the P, P', D, and D' symmetries are calculated with a multiconSguration-interaction wave function. A variation method is used for the bound states whereas the saddle-point and saddle-point complex-rotation methods are used for the autoionizing states. A restricted variation method is used for the saturated wave functions. Fine structures, relativistic corrections, and mass polarization corrections are calculated. The quantum electrodynamic corrections are also estimated. The absolute term energy is predicted with an uncertainty which is much smaller than that in the literature. Among these core-excited states, ten doublet-doublet transitions and one doubletquartet transition have been measured. The largest error bar for the transition energy has been 6.2 cm whereas others range from 0.5 to 3.3 cm . Our predicted transition wavelengths agree with the experiment for 10 of the 11 transitions. The only discrepancy is about 2 cm . In the case where there is a disagreement between different experiments, our results show a clear preference in the comparison. The transition rates calculated in this work suggest that other spectral lines may &iso be observed in future experiments.

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Section: Complex-rotation Calculationmentioning

confidence: 99%

Absolute term energy of core-excited doublet states of lithium

Chen

Chung

1994

Phys. Rev. A

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“…These enzymes catalyze the conjugation of GSH to the electrophilic center of many toxic compounds and also promote GSH-mediated reduction of organic hydroperoxides. In addition, GSTs may act as ligandins for xenobiotics (20) and also as antiapoptotic proteins through protein-protein interaction with Jun kinase (21). Recently, we demonstrated that Alpha, Pi, and Mu class GSTs, which represent 90 -95% of all mammalian GSTs, bind the dinitrosyl-diglutathionyl iron complex with extraordinary high affinity, showing K D values of 10 Ϫ10 -10 Ϫ9 M (9 -11).…”

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confidence: 99%

Glutathione Transferases Sequester Toxic Dinitrosyl-Iron Complexes in Cells

Pedersen¹,

Maria

Turella

et al. 2007

Journal of Biological Chemistry

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It is now well established that exposure of cells and tissues to nitric oxide leads to the formation of a dinitrosyl-iron complex bound to intracellular proteins, but little is known about how the complex is formed, the identity of the proteins, and the physiological role of this process. By using EPR spectroscopy and enzyme activity measurements to study the mechanism in hepatocytes, we here identify the complex as a dinitrosyl-diglutathionyl-iron complex (DNDGIC) bound to Alpha class glutathione S-transferases (

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“…Eight different gene-independent, isoenzymatic classes have been found in mammals, and two of these, Alpha and Mu classes, are abundantly expressed in rat liver, where they represent 43 and 56%, respectively, of the entire pool of cytosolic GSTs (1). Beside their catalytic competence to conjugate GSH to many toxic substances having an electrophilic center, these enzymes also display peroxidase activity and ligandin properties (2,3). In hepatocytes, Alpha GSTs efficiently trap a natural nitric oxide carrier, the dinitrosyl-diglutathionyl-iron complex (DNDGIC), thus preventing the irreversible inhibition of glutathione reductase caused by this compound (4).…”

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confidence: 99%

Electrostatic Association of Glutathione Transferase to the Nuclear Membrane

Stella¹,

Pallottini

Moreno

et al. 2007

Journal of Biological Chemistry

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The possible nuclear compartmentalization of glutathione S-transferase (GST) isoenzymes has been the subject of contradictory reports. The discovery that the dinitrosyl-diglutathionyl-iron complex binds tightly to Alpha class GSTs in rat hepatocytes and that a significant part of the bound complex is also associated with the nuclear fraction (Pedersen, J. Z., De Maria, F., Turella, P., Federici, G., Mattei, M., Fabrini, R., Dawood, K. F., Massimi, M., Caccuri, A. M., and Ricci, G. (2007) J. Biol. Chem. 282, 6364 -6371) prompted us to reconsider the nuclear localization of GSTs in these cells. Surprisingly, we found that a considerable amount of GSTs corresponding to 10% of the cytosolic pool is electrostatically associated with the outer nuclear membrane, and a similar quantity is compartmentalized inside the nucleus. Mainly Alpha class GSTs, in particular GSTA1-1, GSTA2-2, and GSTA3-3, are involved in this double modality of interaction. Confocal microscopy, immunofluorescence experiments, and molecular modeling have been used to detail the electrostatic association in hepatocytes and liposomes. A quantitative analysis of the membrane-bound Alpha GSTs suggests the existence of a multilayer assembly of these enzymes at the outer nuclear envelope that could represent an amazing novelty in cell physiology. The interception of potentially noxious compounds to prevent DNA damage could be the possible physiological role of the perinuclear and intranuclear localization of Alpha GSTs. Glutathione S-transferases (GSTs)2 are a superfamily of enzymes that protect the cell from toxic endogenous or xenobiotic compounds. Eight different gene-independent, isoenzymatic classes have been found in mammals, and two of these, Alpha and Mu classes, are abundantly expressed in rat liver, where they represent 43 and 56%, respectively, of the entire pool of cytosolic GSTs (1). Beside their catalytic competence to conjugate GSH to many toxic substances having an electrophilic center, these enzymes also display peroxidase activity and ligandin properties (2, 3). In hepatocytes, Alpha GSTs efficiently trap a natural nitric oxide carrier, the dinitrosyl-diglutathionyl-iron complex (DNDGIC), thus preventing the irreversible inhibition of glutathione reductase caused by this compound (4). Preliminary evidence was also reported that GSTs could be associated with the nuclear membrane or compartmentalized in nuclei. The presence of GSTs on intracellular membranes is not a new finding. MGST1 is a peculiar trimeric microsomal integral membrane isoenzyme discovered and characterized many years ago (5). GSTA4-4, a specific isoenzyme able to detoxify hydroxyalkenals, displays a widespread mitochondrial, peroxisomal, and cytosolic localization, but the plasma membrane also binds detectable amounts of this enzyme (6). Furthermore, the tight association of Alpha and Mu class GSTs with the microsomal membrane fraction of rat liver was demonstrated by Morgenstern et al. (7), and about 2% of the cytosolic GSTA1-1 has been found in the microsomal membrane...

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On the EUV Spectrum of Li I

Cited by 15 publications

References 15 publications

Absolute term energy of core-excited doublet states of lithium

Absolute term energy of core-excited doublet states of lithium

Glutathione Transferases Sequester Toxic Dinitrosyl-Iron Complexes in Cells

Electrostatic Association of Glutathione Transferase to the Nuclear Membrane

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