Hydrogen bonding/deactivation

The compound 271 or 272 is obtained by dimerization of two radicals (269). It seems that stabilization of the hydrazo derivative through hydrogen bonding deactivates the molecule toward further oxidation. On the other... 

Effect of Temperature and pH. The temperature dependence of enzymes often follows the rule that a 10°C increase in temperature doubles the activity. However, this is only tme as long as the enzyme is not deactivated by the thermal denaturation characteristic for enzymes and other proteins. The three-dimensional stmcture of an enzyme molecule, which is vital for the activity of the molecule, is governed by many forces and interactions such as hydrogen bonding, hydrophobic interactions, and van der Waals forces. At low temperatures the molecule is constrained by these forces as the temperature increases, the thermal motion of the various regions of the enzyme increases until finally the molecule is no longer able to maintain its stmcture or its activity. Most enzymes have temperature optima between 40 and 60°C. However, thermostable enzymes exist with optima near 100°C. 

Thus it seems clear that, in the absence of interactions with the reaction medium, SOR groups behave as — R substituents and activate electrophilic substitution. However, they are prone to protonation or at least to act as hydrogen bond acceptors, in which condition they behave as + R substituents, deactivate electrophilic substitution and are metadirecting. 

The original stabilizer (HBC) was modified as the rapid radiationless deactivation of the stabilizer is (at least partly) due to the intramolecular hydrogen bond, the H-atom was substituted by a methyl group (MBC). This "probe molecule" showed fluorescence and phosphorescence and enabled us to demonstrate the energy transfer to the stabilizer, simply by studying its sensitized luminescence. 

While we used the probe molecule to investigate the energy transfer by sensitized phosphorescence we now turn to the stabilizer itself (e.g. TIN with an intramolecular hydrogen bond) to study its deactivation in the excited states. 

The internal hydrogen bond is the origin of the rapid deactivation. 

Partial rate factors for the sulphonation of compounds Phfd-E), NO2 have been measured227, n being 0, 2 or 3. This is another system in which the ortho position is deactivated more than the para. Under the highly acidic conditions used it seems likely that the effective substituent is the hydrogen-bonded or even protonated group. 

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