Related Experiment Video
Updated: Jul 16, 2026

Light-driven Enzymatic Decarboxylation
Published on: May 22, 2016
Inactivation of acetyl-CoA synthase/carbon monoxide dehydrogenase by copper
Matthew R Bramlett1, Xiangshi Tan, Paul A Lindahl
1Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, USA.
Abstract:
Two recent crystal structures of acetyl-CoA synthase (ACS) from Moorella thermoacetica exhibited different metal contents and geometries at their active site, called the A-cluster. This led to the proposal of two catalytic mechanisms, one Ni-based, the other Cu-based. ACS was studied with respect to synthase activity, methyl group transfer activity, metal content, and EPR spectroscopy. Our results indicate that Cu is not required for catalysis and that it inactivates ACS by binding to the proximal site of the A-cluster. With Cu in this site, the A-cluster cannot accept a methyl group from the corrinoid-iron-sulfur protein, nor can it exhibit the NiFeC EPR signal after treatment with CO.
More Related Videos
Related Concept Videos
Pyruvate Oxidation
First, the enzyme pyruvate dehydrogenase removes the carboxyl group from pyruvate and releases it as carbon dioxide. The stripped molecule is then oxidized and releases electrons, which are then picked up by NAD+...
Oxidative Cleavage of Alkenes: Ozonolysis
Ozone is a symmetrical bent molecule stabilized by a resonance structure.
Fates of Pyruvate
In aerobic organisms, pyruvate is metabolized via the citric acid cycle to produce reduced coenzymes NADH and FADH2. These coenzymes are then oxidized in the electron transport chain to produce ATP and, in the process, regenerate the NAD+ and FAD. As seen in some cell types and organisms, fermentation...
Loss of Carboxy Group as CO2: Decarboxylation of β-Ketoacids
Phase I Oxidative Reactions: Overview
Respiration Pathways

