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Electron paramagnetic resonance iron complexes

Pellat, C., Henry, Y., and Drapier, j. C. (1990). IFN-gamma-activated macrophages Detection by electron paramagnetic resonance of complexes between L-arginine-derived nitric oxide and nonheme iron proteins. Biochem. Biophys. Res. Commun. 166, 119-125. [Pg.172]

One of the earliest reports of LO inhibition concerned the effects of ortho-dihydroxybenzene (catechol) derivatives on soybean 15-LO [58]. Lipophilic catechols, notably nordihydroguaiaretic acid (NDGA) (19), were more potent (10 /zM) than pyrocatechol itself. The inactivation was, under some conditions, irreversible, and was accompanied by oxidation of the phenolic compound. The orfAo-dihydroxyphenyl moiety was required for the best potency, and potency also correlated with overall lipophilicity of the inhibitor [61]. NDGA and other phenolic compounds have been shown by electron paramagnetic resonance spectroscopy to reduce the active-site iron from Fe(III) to Fe(II) [62] one-electron oxidation of the phenols occurs to yield detectable free radicals [63]. Electron-poor, less easily oxidized catechols form stable complexes with the active-site iron atom [64]. [Pg.8]

Henry, Y., Ducrocq, C., Drapier, J. C., Servent, D., Pellat, C., and Guissani, A. (1991). Nitric oxide, a biological effector. Electron paramagnetic resonance detection of nitrosyl-iron-protein complexes in whole cells. Eur. Biophys. J. 20, 1-15. [Pg.168]

Stadler, J., Bergonia, H. A., Di Silvio, M., Sweetland, M. A., Billiar, T. R., Simmons, R. L., and Lancaster, J. R., Jr. (1993). Nonheme iron-nitrosyl complex formation in rat hepatocytes Detection by electron paramagnetic resonance spectroscopy. Arch. Biochem. Biophys. 302, 4-11. [Pg.173]

Windle, J. J., A. L. Wiersema, J. R. Clark, and R. E. Feeney Investigation of the iron and copper complexes of avian conalbumins and human transferrins by electron paramagnetic resonance. Biochemistry 2, 1341 (1963). [Pg.206]

Electron paramagnetic resonance (EPR) spectroscopy is a powerful technique to explore the electronic state of iron complexes. EPR spectroscopy of the non-heme iron component in the electron transfer system of mitochondria has been extensively used and discussed by Beinert (9), who showed that this type of iron has a so-called g = 1.94 type signal upon reduction. Consideration of the EPR spectrum of adrenodoxin has been described previously (68). [Pg.18]

Abbreviations FAD, flavin adenine dinucleotide Fe-S, iron-sulfur proteins that can he identified in separate clusters by electron paramagnetic resonance analysis (the s-1, s-2 subscripts identify these iron-sulfur proteins as part of the succinate dehydrogenase complex) His, the histidine linkage between FAD and the large (70,000 daltons) protein moiety of the enzyme FMN, flavin mononucleotide N-la, N-2 subscripts identify these iron-sulfur proteins as part of the NADH-dehydro-genase complex UQ, ubiquinone Cyt bf and Cyt b, cytochrome b-566 and b-563, respectively. [Pg.180]

JS Rieske, WS Zaugg and RE Hansen (1964) Studies on the electron transfer system. LIX. Distribution of iron and of the component giving an electron paramagnetic resonance signal at g= 1.90 in subtractions of complex III. J Bioi Chem 239 3017-3022... [Pg.662]


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See also in sourсe #XX -- [ Pg.185 , Pg.186 ]




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Electron paramagnetic

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