Heavy atom nitroxyl radicals. II: Spectroscopic detection of H2As=O, the prototypical arsenyl free radical

2009 ◽  
Vol 131 (11) ◽  
pp. 114311 ◽  
Author(s):  
Sheng-Gui He ◽  
Fumie X. Sunahori ◽  
Jie Yang ◽  
Dennis J. Clouthier
Keyword(s):  
Free Radical ◽  
Heavy Atom ◽  
Nitroxyl Radicals

Heavy atom nitroxyl radicals. V. An experimental andab initiostudy of the previously unknown H2PS free radical

2011 ◽  
Vol 135 (21) ◽  
pp. 214306 ◽  
Author(s):  
Robert A. Grimminger ◽  
Dennis J. Clouthier ◽  
Riccardo Tarroni
Keyword(s):  
Free Radical ◽  
Heavy Atom ◽  
Nitroxyl Radicals

Heavy atom nitroxyl radicals. VI. The electronic spectrum of jet-cooled H2PO, the prototypical phosphoryl free radical

2011 ◽  
Vol 135 (21) ◽  
pp. 214307 ◽  
Author(s):  
Mohammed A. Gharaibeh ◽  
Dennis J. Clouthier ◽  
Riccardo Tarroni
Keyword(s):  
Free Radical ◽  
Electronic Spectrum ◽  
Heavy Atom ◽  
Nitroxyl Radicals

scholarly journals Sodium nitrite and ascorbic acid: a metal-free combination that controls the free-radical polymerization of tert-butyl methacrylate in water

e-Polymers ◽  
2002 ◽  
Vol 2 (1) ◽  
Author(s):  
Christophe Detrembleur ◽  
Ange Mouithys-Mickalad ◽  
Philippe Teyssié ◽  
Robert Jérôme
Keyword(s):  
Nitric Oxide ◽  
Ascorbic Acid ◽  
Free Radical ◽  
Radical Polymerization ◽  
Sodium Nitrite ◽  
Free Radical Polymerization ◽  
Nitroxyl Radicals ◽  
Butyl Methacrylate ◽  
Metal Free ◽  
Tert Butyl

AbstractA mixture of sodium nitrite and ascorbic acid is able to control the radical polymerization of tert-butyl methacrylate (tBMA) in water at 80°C. Indeed, sodium nitrite is reduced by the ascorbic acid, and the nitric oxide (NO) which is formed insitu is nothing but a promoter of nitroxyl radicals. The radical polymerization of tBMA is thus basically controlled by a nitroxide-mediated process.

Pt(II)-, Pd(II)-und Cu(II)-Komplexe mit dem 4.4.5.5-Tetramethylimidazolin-1-oxyl-2-m-pyridyl-3-oxid-Liganden / Pt(II), Pd(II) and Cu(II) Complexes with the Ligand 4,4,5,5-Tetramethylimidazohne-1-oxyl-2-m-pyridyl-3-oxide

1981 ◽  
Vol 36 (2) ◽  
pp. 195-197 ◽  
Author(s):  
Karl E. Schwarzhans ◽  
Alfons Stuefer
Keyword(s):  
Free Radical ◽  
Magnetic Moments ◽  
Nitroxyl Radicals ◽  
Epr Spectra ◽  
Stable Free Radical

Abstract The stable free radical 4,4,5,5-tetramethylimidazoline-1-oxyl-2-m-pyridyl-3-oxide has been prepared and used as a ligand in platinum(II), palladium(II) and copper(II) complexes. The magnetic moments and the EPR spectra of the complexes and the free radical have been investigated. The complexes show a considerable interaction between the nitroxyl radicals of the ligands.

Heavy atom effects on geminate and free radical recombination

1988 ◽  
Vol 45 (1) ◽  
pp. 1-7 ◽  
Author(s):  
Koichi Kikuchi ◽  
Masato Hoshi ◽  
Etsuko Abe ◽  
Hiroshi Kokubun
Keyword(s):  
Free Radical ◽  
Heavy Atom ◽  
Radical Recombination

Isomorphous replacement in electron diffraction of wet crystals of rat hemoglobin

1983 ◽  
Vol 41 ◽  
pp. 446-447
Author(s):  
William F. Tivol ◽  
Murray Vernon King ◽  
D. F. Parsons
Keyword(s):  
Electron Diffraction ◽  
Heavy Atom ◽  
Isomorphous Substitution ◽  
X Ray Diffraction ◽  
Salt Solutions ◽  
X Ray ◽  
Isomorphous Replacement ◽  
Structure Factors ◽  
Diffraction Structure ◽  
The Mean

Feasibility of isomorphous substitution in electron diffraction is supported by a calculation of the mean alteration of the electron-diffraction structure factors for hemoglobin crystals caused by substituting two mercury atoms per molecule, following Green, Ingram & Perutz, but with allowance for the proportionality of f to Z3/4 for electron diffraction. This yields a mean net change in F of 12.5%, as contrasted with 22.8% for x-ray diffraction.Use of the hydration chamber in electron diffraction opens prospects for examining many proteins that yield only very thin crystals not suitable for x-ray diffraction. Examination in the wet state avoids treatments that could cause translocation of the heavy-atom labels or distortion of the crystal. Combined with low-fluence techniques, it enables study of the protein in a state as close to native as possible.We have undertaken a study of crystals of rat hemoglobin by electron diffraction in the wet state. Rat hemoglobin offers a certain advantage for hydration-chamber work over other hemoglobins in that it can be crystallized from distilled water instead of salt solutions.

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