Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1269592 | Bioelectrochemistry | 2006 | 4 Pages |
Abstract
The change in the energy barriers for the heterogeneous reduction of pyruvate decarboxylase (PDC) relative to its coenzyme, thiamin pyrophosphate (ThPP), was determined experimentally using square wave voltammetry (SWV) to be 5.3 kcal/mol. These results are in agreement with those of reaction rate acceleration provided by thiamin-dependent decarboxylases relative to their coenzyme as determined kinetically based on the pKa suppression by the enzyme environment.
Related Topics
Physical Sciences and Engineering
Chemistry
Electrochemistry
Authors
Patrick Bell, Kathryn Hoyt, Masangu Shabangi,