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Author Seltzer, S. ♦ Hamilton, G. A. ♦ Westheimer, F. H.
Sponsorship USDOE
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword CHEMISTRY ♦ CATALYSIS ♦ CATIONS ♦ CHEMICAL REACTIONS ♦ DECOMPOSITION ♦ ENZYMES ♦ HEAVY WATER ♦ ISOTOPE EFFECTS ♦ MANGANESE COMPOUNDS ♦ ORGANIC ACIDS ♦ OXALIC ACID ♦ PRODUCTION ♦ REACTION KINETICS ♦ WATER
Abstract HO/sub 2/C --CO-- CH/sub 2/-- C/sup 13/O/sub 2/H has been prepared and decarboxylated in the presence of metal ions and in the presence of the partially purified enzyme from Micrococcus lysodeikticus. The reaction catalyzed by Microat 10 deg showed an isotope effect, k/sup 12//k/sup 13/, of nearlty 1.06, whereas the ratio for the enzymatic reaction was 1.00. Further, the enzymatic decarboxylation proceeds less rapidly in D/sub 2/O than in H/sub 2/O, whereas the rate for the metal ion-promoted reaction is unaffected by this change in solvent. These facts show that the carbon--carbon bond scission is the rate-controlling process for the non-enzymatic reaction but not for that promoted by the enzyme. The actual rates make it probable that the carbon--carbon bond cleavage for the enzymatic reaction exceeds that for the non-enzymatic reaction by a factor of the order of 10/sup 8/. (auth)
ISSN 00027863
Educational Use Research
Learning Resource Type Article
Publisher Date 1959-08-01
Publisher Department Harvard Univ., Cambridge, Mass.
Journal Journal of the American Chemical Society
Volume Number 81
Organization Harvard Univ., Cambridge, Mass.


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