ORGN 676 |
| Peptidylglycine amidating-amidating monooxygenase catalyzes the formation and breakdown of carbinolamides. Very little is known about method of catalysis used by the lyase portion of the enzyme. It is generally accepted that carbinolamides breakdown by specific-acid/base mechanisms which would not be conducive to the usual general-acid/base mechanisms employed by enzymes. We report the second-order rate constants for the general buffer catalyzed breakdown of N-(hydroxymethyl)benzamide (1) in water at 25oC, I = 1.0 (KCl) by pivalic, acetic, chloroacetic and dichloroacetic acid. The observed rate increased with increasing amounts of the acidic form of the buffer and a BrØnsted correlation of –alpha = -0.41 was found. The results presented here represent the first evidence of a buffer catalyzed reaction for the aqueous reaction of 1 and for carbinolamides in general. |
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Physical Organic Chemistry: Calculations, Mechanisms, Photochemistry, and High-Energy Species
1:00 PM-5:00 PM, Wednesday, 16 March 2005 Convention Center -- Room 11A, Oral
Division of Organic Chemistry |