@article {1121,
	title = {Theoretical studies of alkyl radicals in the NaY and HY zeolites},
	journal = {J. Phys. Chem. A},
	volume = {109},
	number = {32},
	year = {2005},
	note = {ISI Document Delivery No.: 954TRTimes Cited: 8Cited Reference Count: 68},
	month = {Aug},
	pages = {7242-7250},
	type = {Article},
	abstract = {<p>Interplay of quantum mechanical calculations and experimental data on hyperfine coupling constants of ethyl radical in zeolites at several temperatures was engaged to study the geometries and binding energies and to predict the temperature dependence of hyperfine splitting of a series of alkyl radicals in zeolites for the first time. The main focus is on the hyperfine interaction of alkyl radicals in the NaY and HY zeolites. The hyperfine splitting for neutral free radicals and free radical cations is predicted for different zeolite environments. This information can be used to establish the nature of the muoniated alkyl radicals in the NaY and HY zeolites via mu SR experiments. The ration hyperfine coupling constants of the ethane radical cation in these zeolites are very large with relatively little dependence on temperature. It was found that the intramolecular dynamics of alkyl free radicals are only weakly affected by their strong binding to zeolites. In contrast, the substrate binding has a significant effect on their intermolecular dynamics.</p>},
	keywords = {CYCLOHEXADIENYL RADICALS, DENSITY-FUNCTIONAL CALCULATIONS, ELECTRON-SPIN-RESONANCE, ethyl, GAS-PHASE, HYPERFINE COUPLING-CONSTANTS, INTERNAL-ROTATION, INTRAMOLECULAR MOTION, METHYL, REORIENTATIONAL DYNAMICS},
	isbn = {1089-5639},
	url = {<Go to ISI>://000231178300029},
	author = {K. Ghandi* and Zahariev, F. E. and Wang, Y. A.}
}
@article {5225,
	title = {Reaction of human myoglobin and nitric oxide - Heme iron or protein sulfhydryl (S) nitrosation dependence on the absence or presence of oxygen},
	journal = {Journal of Biological Chemistry},
	volume = {276},
	number = {6},
	year = {2001},
	note = {ISI Document Delivery No.: 401HBTimes Cited: 33Cited Reference Count: 58},
	month = {Feb},
	pages = {3991-3998},
	type = {Article},
	abstract = {The amino acid sequence of human myoglobin (Mb) is similar to other mammalian Mb except for a unique cysteine residue at position 110 (Cys(110)). Anaerobic treatment of ferrous forms of wild-type human Rib, the C110A variant of human Mb or horse heart Mb, with either authentic NO or chemically derived NO in vitro yields heme-NO complexes as detected by electron paramagnetic resonance spectroscopy (EPR). By contrast, no EPR-detectable heme-NO complex was observed from the aerobic reactions of NO and either the ferric or oxy-Mb forms of wild-type human or horse heart myoglobins, Mass analyses of wild-type human Mb treated aerobically with NO indicated a mass increase of similar to 30 atomic mass units (i.e,, NO/Mb = 1 mol/mol), Mass analyses of the corresponding apoprotein after heme removal showed that NO was associated with the apoprotein fraction. New electronic maxima were detected at A(333) nm (epsilon = 3665 +/- 90 mol(-1) cm(-1); mean +/- S.D.) and A(545) nm (epsilon = 44 +/- 3 mol(-1) cm(-1)) in solutions of S-nitrosated wild-type human Mb (similar to S-nitrosoglutathione), Importantly, the sulfhydryl S-H stretch vibration for Cys(110) measured by Fourier transform infrared (nu similar to 2552 cm(-1)) was absent for both holo- and apo- forms of the wild-type human protein after aerobic treatment of the protein with NO. Together, these data indicate that the reaction of wild-type human Mb and NO yields either heme-NO or a novel S-nitrosated protein dependent on the oxidation state of the heme iron and the presence or absence of dioxygen.},
	keywords = {ELECTRON-SPIN-RESONANCE, GLUTATHIONE, HEMOGLOBIN, HUMAN SKELETAL-MUSCLE, METMYOGLOBIN, NITROSOTHIOLS, OXIDATION, RELAXING FACTOR, SMOOTH-MUSCLE, VASCULAR TONE},
	isbn = {0021-9258},
	url = {<Go to ISI>://000166921200038},
	author = {Witting, P. K. and Douglas, D. J. and Mauk, A. G.}
}
@article {3125,
	title = {RADICAL FORMATION DURING THE REACTION OF BIS(FLUOROSULFURYL)PEROXIDE, S2O6F2, WITH TETRASULFUR TETRANITRIDE, S4N4, AND ELEMENTAL SULFUR, S-8},
	journal = {Journal of Fluorine Chemistry},
	volume = {66},
	number = {2},
	year = {1994},
	note = {ISI Document Delivery No.: MX367Times Cited: 1Cited Reference Count: 46},
	month = {Feb},
	pages = {147-152},
	type = {Article},
	abstract = {The radical intermediates formed initially in the reaction of S2O6F2 with S4N4 and S8 have been studied by ESR spectroscopy at X-band level. The transient radical formed in the reaction between S2O6F2 and S4N4 has the spin Hamiltonian parameters g(xx) = 2.0014, g(yy) = 2.0054, g(zz) = 2.0249, A(xx) = 22.5 MHz, A(yy) = 4.5 MHz, A(zz) = 2.0 MHz and Q(zz) = 4 MHz as determined by simulation of ESR lineshapes obtained from polycrystalline samples. The spin Hamiltonian parameters are very similar to those previously reported for [S3N2]+., and the spectra are interpreted as being most likely due to the [S3N2]+. radical. The reaction between S2O6F2 and S8 under similar conditions produces a radical that has a g-tensor of the form g(xx) = 2.0026, g(yy) = 2.0184, g(zz) = 2.0258, as determined by simulation. The transient species generated is postulated to be a similar S5+. radical.},
	keywords = {CRYSTAL-STRUCTURE, ELECTRON-SPIN-RESONANCE, HSO3F, NITROGEN, POLYATOMIC CATIONS, S3N2+, SALTS, SPECTRUM},
	isbn = {0022-1139},
	url = {<Go to ISI>://A1994MX36700011},
	author = {Mistry, F. and Herring, F. G. and Haas, A. and Aubke, F.}
}
