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Di-oxygen molecule

Stable Free Radicals. Stable free radicals are a small minority of the more than 6 million chemical compounds known by 2005. The oxygen molecule is paramagnetic (S = 1). In 1896, Ostwald stated that "free radicals cannot be isolated." Only four years later, Gomberg123 made triphenylmethyl (Fig. 11.63), the first proven stable and persistent free radical [48] An infinitely stable free radical used as a reference in EPR is diphenyl-picryl hydrazyl (DPPH). Other persistent free radicals are Fremy s124 salt (dipotassium nitrosodisulfonate K+ O3S-NO-SO3- K+) 2,2-diphenyl-l-picrylhydrazy (DPPH)l, Galvinoxyl (2,6-di-tert-butyl-a-(3,5-di-tert-butyl-4-oxo-2,5-cyclohexadien-l-ylidene)-p-... [Pg.725]

If the body cells require instant energy (as in exercise), the glucose is supplied with oxygen from the blood and is immediately oxidized on the instructions of a facilitating ADP (adenosine di-phosphate) molecule to release energy ... [Pg.61]

Classical simulations are used to examine the transport of di-oxygen across to the active site of the heme protein. An expansion was not used, and dilferent scanning times and agreement of the profiles were used to assess the convergence of the results. Vemparala et alP use the JE and methods based on the JE to examine the transport of a halothane molecule across a lipid/water interface. [Pg.199]

The possible origins of irreversible capacity have been carefully studied by a number of authors. Some papers claim that lithium could be irreversibly trapped by the surface functional groups of carbon [23], e.g., by electrostatic forces such as —COO Li, or that it could react with di-oxygen or water molecules adsorbed on the carbon surface [24]. A linear dependence has been found between the irreversible capacity of a series of carbons and their micropore volume [25], and Li NMR experiments lead to the conclusion that metallic... [Pg.597]

When composite resins undergo polymerization, a thin layer exposed to the air fails to react. This is due to the presence of oxygen. The oxygen molecule is a di-radical, that is, it has two unpaired electrons. This makes it reactive towards the free radicals within the setting composite, and it reacts readily with these free radicals to form unreactive... [Pg.44]

Hydrogen peroxide, H2O2, together with organic peroxides, is involved in a number of biological pathways, where this molecule is frequently monitored, but also plays an important role in many industrial processes. Last but not least, the environmental importance of (di)oxygen, O2, is obvious and does not need any special comment, perhaps, a remark that, in envirramiental determinations by electrochemical methods, the respective procedures are predominantly dealing with its determination in water samples. [Pg.126]

Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)... Figure 1.9 Examples of functionally important intrinsic metal atoms in proteins, (a) The di-iron center of the enzyme ribonucleotide reductase. Two iron atoms form a redox center that produces a free radical in a nearby tyrosine side chain. The iron atoms are bridged by a glutamic acid residue and a negatively charged oxygen atom called a p-oxo bridge. The coordination of the iron atoms is completed by histidine, aspartic acid, and glutamic acid side chains as well as water molecules, (b) The catalytically active zinc atom in the enzyme alcohol dehydrogenase. The zinc atom is coordinated to the protein by one histidine and two cysteine side chains. During catalysis zinc binds an alcohol molecule in a suitable position for hydride transfer to the coenzyme moiety, a nicotinamide, [(a) Adapted from P. Nordlund et al., Nature 345 593-598, 1990.)...
C13HuC1N307 2,2 -Anhydro-[5-chloro-l-(3,5-di-0-acetyl-/ -D-arabino-furanosyl)-6-oxocytosine] (ACAFCC)166 I4t Z — 8 D = 1.56 R = 0.066 for 818 intensities. The glycosyl disposition of the anhydronucleoside is constrained to the syn (— 68.8°) orientation. The conformation of the D-arabinofuranosyl group is a flattened 4E (232.6°, 18.0°), and the exocyclic, C-4 -C-5 bond torsion-angle is g auche+ (50.2°). The adjacent bases are connected by N-H O hydrogen-bonds between the N-4 atom of one molecule and the carbonyl oxygen atom (0-4) of another. The twofold-symmetry-related bases are stacked, with an interbase separation of 329 pm. [Pg.292]


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See also in sourсe #XX -- [ Pg.10 , Pg.11 ]

See also in sourсe #XX -- [ Pg.10 , Pg.11 ]




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