Catalytic recruitment by phosphonyl derivatives as inactivators of acetylcholinesterase and substrates for imidazole-catalyzed hydrolysis: .beta.-deuterium isotope effects

beta -Deuterium secondary isotope effects for the phosphonylation of the active site serine of acetylcholinesterase (AChE) by phosphonyl derivatives at 25 degree C and pH 7.70 in 0.05 M phosphate buffer are described in this report. The results indicate an increase in the force constants for the CL...

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Published inJournal of the American Chemical Society Vol. 111; no. 16; pp. 6424 - 6427
Main Authors Bennet, Andrew J, Kovach, Ildiko M, Bibbs, Jeffrey A
Format Journal Article
LanguageEnglish
Published Washington, DC American Chemical Society 01.08.1989
Subjects
Chemistry
deuterium
Exact sciences and technology
Labelled compounds chemistry
Organic chemistry
Reactivity and mechanisms
Deuterium
Hydrolysis
Catalytic reaction
Isotope effect
Hydrogen Isotopes
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Summary:beta -Deuterium secondary isotope effects for the phosphonylation of the active site serine of acetylcholinesterase (AChE) by phosphonyl derivatives at 25 degree C and pH 7.70 in 0.05 M phosphate buffer are described in this report. The results indicate an increase in the force constants for the CL (L = H, D) bonds adjacent to phosphorus at the transition state for phosphonylation. This trend is pronounced in the AChE reaction, conceivably due to a more compressed structure at the transition state for the AChE reaction in comparison to the imidazole-catalyzed hydrolysis of the phosphonyl derivatives.
Bibliography:ark:/67375/TPS-PSHV1XZ3-T
istex:01A314225D0FE8C119F7B630CF3338F2C312B48C
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0002-7863
1520-5126
DOI:10.1021/ja00198a067