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Acid Radical (acid + radical)
Selected AbstractsFatty acids increase the circulating levels of oxidative stress factors in mice with diet-induced obesity via redox changes of albuminFEBS JOURNAL, Issue 15 2007Mayumi Yamato Plasma concentrations of free fatty acids are increased in metabolic syndrome, and the increased fatty acids may cause cellular damage via the induction of oxidative stress. The present study was designed to determine whether the increase in fatty acids can modify the free sulfhydryl group in position 34 of albumin (Cys34) and enhance the redox-cycling activity of the copper,albumin complex in high-fat diet-induced obese mice. The mice were fed with commercial normal diet or high-fat diet and water ad libitum for 3 months. The high-fat diet-fed mice developed obesity, hyperlipemia, and hyperglycemia. The plasma fatty acid/albumin ratio also significantly increased in high-fat diet-fed mice. The increased fatty acid/albumin ratio was associated with conformational changes in albumin and the oxidation of sulfhydryl groups. Moreover, an ascorbic acid radical, an index of redox-cycling activity of the copper,albumin complex, was detected only in the plasma from obese mice, whereas the plasma concentrations of ascorbic acid were not altered. Plasma thiobarbituric acid reactive substances were significantly increased in the high-fat diet group. These results indicate that the increased plasma fatty acids in the high-fat diet group resulted in the activated redox cycling of the copper,albumin complex and excessive lipid peroxidation. [source] Multi-frequency EPR and Mössbauer spectroscopic studies on freeze-quenched reaction intermediates of nitric oxide synthase ,MAGNETIC RESONANCE IN CHEMISTRY, Issue S1 2005C. Jung Abstract It is believed by analogy to chloroperoxidase (CPO) from Caldariomyces fumago that the electronic structure of the intermediate iron-oxo species in the catalytic cycle of nitric oxide synthase (NOS) corresponds to an iron(IV) porphyrin- , -cation radical. Such species can also be produced by the reaction of ferric NOS with external oxidants within the shunt pathway. We present multi-frequency EPR (9.6, 94, 285 GHz) and Mössbauer spectroscopic studies on freeze-quenched intermediates of the oxygenase domain of nitric oxide synthase which has reacted with peroxy acetic acid within 8,200 ms. The intermediates of the oxygenase domain of both the cytokine inducible NOS (iNOSox) and the neuronal NOS (nNOSox) show an organic radical signal in the 9.6-GHz spectrum overlapping with the spectrum of an unknown species with g -values of 2.24, 2.23 and 1.96. Using 94- and 285-GHz EPR the organic radical signal is assigned to a tyrosine radical on the basis of g -values (i.e. Tyr*562 in nNOSox and Tyr*341 in iNOSox). Mössbauer spectroscopy of 57Fe-labeled unreacted nNOSox shows a ferric low-spin heme-iron (, = 0.38 mms,1, ,EQ = 2.58 mms,1). The reaction of nNOSox with peroxy acetic acid for 8 ms leads to the disappearance of the magnetic background characteristic for native nNOSox and a new species with , = 0.27 mms,1 and ,EQ = 2.41 mms,1 is detected at 4.2 K which does not resemble the parameters typical for a Fe(IV) center. It is proposed that this intermediate species corresponds to a ferric low-spin species which magnetically couples to an amino acid radical (presumably Trp*409). Copyright © 2005 John Wiley & Sons, Ltd. [source] The g -values and hyperfine coupling of amino acid radicals in proteins: comparison of experimental measurements with ab initio calculations,MAGNETIC RESONANCE IN CHEMISTRY, Issue S1 2005Sun Un Abstract Electron paramagnetic resonance (EPR) spectroscopy has been extensively used to identify and characterize protein-based redox active amino acid radicals based on their g -values and hyperfine couplings. To better understand how these parameters depend on the electronic structure and environment of the radical, the theoretical g -values and proton hyperfine tensors of three models corresponding to the tyrosyl, tryptophanyl and glycyl radicals were calculated using Gaussian 03. The g -values were determined using the B3LYP/6,31+G(D,P) combination of density functional and basis set, while the hyperfine tensors were determined using the B3LYP/EPR-III and PBE0/EPR-III combinations. Comparisons are made to measured values. It was found that by appropriately accounting for hydrogen bonds and the dielectric constant of the environment, good agreement could be achieved between the calculated and measured g -values. In all three cases, the g -anisotropy arose from significant spin density on a nitrogen or oxygen atom. The calculated hyperfine tensors for the three radicals did not differ significantly from previous calculations. In the case of the tyrosyl radical, it is shown for the first time that the para -position substituent that is opposite of the CO group can break the symmetry of the phenyl ring, leading to different hyperfine tensors for the two large ortho proton couplings. For the tyrosyl and tryptophanyl models, the calculated hyperfine couplings to hydrogen-bonding protons were in very good agreement with measured values for both the tyrosyl and tryptophanyl models. Copyright © 2005 John Wiley & Sons, Ltd. [source] | ||||||||||