44 resultados para Electron-Cyclotron Resonance
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Acc. Chem. Res., 2006, 39 (10), pp 788–796 DOI: 10.1021/ar050104k
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The most important processes for the creation of S12+ to S14+ ions excited states from the ground configurations of S9+ to S14+ ions in an electron cyclotron resonance ion source, leading to the emission of K X-ray lines, are studied. Theoretical values for inner-shell excitation and ionization cross sections, including double KL and triple KLL ionization, transition probabilities and energies for the deexcitation processes, are calculated in the framework of the multi-configuration Dirac-Fock method. With reasonable assumptions about the electron energy distribution, a theoretical K$\alpha$ X-ray spectrum is obtained, which is compared to recent experimental data.
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Proceedings of the Chemistry and Conservation Science
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Background/Aims: Unconjugated bilirubin (UCB) impairs crucial aspects of cell function and induces apoptosis in primary cultured neurones. While mechanisms of cytotoxicity begin to unfold, mitochondria appear as potential primary targets. Methods: We used electron paramagnetic resonance spectroscopy analysis of isolated rat mitochondria to test the hypothesis that UCB physically interacts with mitochondria to induce structural membrane perturbation, leading to increased permeability, and subsequent release of apoptotic factors. Results: Our data demonstrate profound changes on mitochondrial membrane properties during incubation with UCB, including modified membrane lipid polarity and fluidity (P , 0:01), as well as disrupted protein mobility(P , 0:001). Consistent with increased permeability, cytochrome c was released from the intermembrane space(P , 0:01), perhaps uncoupling the respiratory chain and further increasing oxidative stress (P , 0:01). Both ursodeoxycholate, a mitochondrial-membrane stabilising agent, and cyclosporine A, an inhibitor of the permeability transition, almost completely abrogated UCB-induced perturbation. Conclusions: UCB directly interacts with mitochondria influencing membrane lipid and protein properties, redox status, and cytochrome c content. Thus, apoptosis induced by UCB may be mediated, at least in part, by physical perturbation of the mitochondrial membrane. These novel findings should ultimately prove useful to our evolving understanding of UCB cytotoxicity.
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Dissertation presented to obtain the PhD degree in Biochemistry
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J Biol Inorg Chem (2011) 16:443–460 DOI 10.1007/s00775-010-0741-z
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J Biol Inorg Chem (2008) 13:1321–1333 DOI 10.1007/s00775-008-0416-1
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J Biol Inorg Chem. 2008 Jun;13(5):737-53. doi: 10.1007/s00775-008-0359-6
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J Biol Inorg Chem (2007) 12:777–787 DOI 10.1007/s00775-007-0229-7
Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase
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J Biol Inorg Chem (2007) 12:353–366 DOI 10.1007/s00775-006-0191-9
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J Biol Inorg Chem (2006) 11: 609–616 DOI 10.1007/s00775-006-0110-0
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Biochemistry. 2008 Oct 14;47(41):10852-62. doi: 10.1021/bi801375q
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Dissertação para obtenção do Grau de Doutor em Bioquímica, ramo de Biotecnologia
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FEBS Letters 579 (2005) 4585–4590
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Journal of Electroanalytical Chemistry 541 (2003) 153-162