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The gauche effect is very sensitive to solvent effects, due to the large difference in polarity between the two conformers.For example, 2,3-dinitro-2,3-dimethylbutane, which in the solid state exists only in the gauche conformation, prefers the gauche conformer in benzene solution by a ratio of 79:21, but in carbon tetrachloride, it prefers the anti conformer by a ratio of 58:42. [9]
The two have equal free energy; neither is more stable, so neither predominates compared to the other. A negative difference in free energy means that a conformer interconverts to a thermodynamically more stable conformation, thus the equilibrium constant will always be greater than 1.
Peroxidase, a heme-containing oxidoreductase, is a commercially important enzyme which catalyses the reductive cleavage of hydrogen peroxide by an electron donor. Horseradish peroxidase is ideal in many respects for these applications because it is smaller, more stable, and less expensive than other popular alternatives such as alkaline ...
In the initiation phase, a pro-oxidant hydroxyl radical (OH•) abstracts the hydrogen at the allylic position (–CH 2 –CH=CH 2) or methine bridge (=CH−) [clarification needed] on the stable lipid substrate, typically a polyunsaturated fatty acid (PUFA), to form the lipid radical (L•) and water (H 2 O).
More complex molecules, such as butane, have more than one possible staggered conformation. The anti conformation of butane is approximately 0.9 kcal mol −1 (3.8 kJ mol −1) more stable than the gauche conformation. [1] Both of these staggered conformations are much more stable than the eclipsed conformations.
In nonpolar solvents, a range between 0.2 and 0.6 kcal/mol has been estimated, but in polar solvents the axial conformer may be more stable. [21] The two conformers interconvert rapidly through nitrogen inversion ; the free energy activation barrier for this process, estimated at 6.1 kcal/mol, is substantially lower than the 10.4 kcal/mol for ...
Glutathione peroxidase 1 (GPx1) is the most abundant version, found in the cytoplasm of nearly all mammalian tissues, whose preferred substrate is hydrogen peroxide. Glutathione peroxidase 4 (GPx4) has a high preference for lipid hydroperoxides; it is expressed in nearly every mammalian cell, though at much lower levels.
Hydroperoxides are much less reactive than the peroxyacids. [2] The use of hydrogen peroxide even requires a catalyst. [7] [20] In addition, using organic peroxides and hydrogen peroxide often promotes side-reactions. [21] Oxygen can be used to convert cyclohexanol to caprolactone, but the process generates hydrogen peroxide in situ: [7]