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![[DPEPhosbcpCu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F59739.jpg&w=3840&q=50)
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[DPEPhosbcpCu]PF6: A General and Broadly Applicable Copper-Based Photoredox Catalyst
Published on: May 21, 2019
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Copper Activates a Redox Switch to Reversibly Inhibit Glyceraldehyde-3-Phosphate Dehydrogenase.
Taylor C Outlaw1, Amy T R Robison1, Natalie B Schulte1
1Department of Chemistry, Duke University, Durham, North Carolina 27708, United States of America.
Biochemistry
|October 23, 2025
Summary
Metal ions like copper and silver can reversibly inactivate Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), turning it into a cellular redox switch. This protects cells from toxic metals and reactive oxygen species.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a highly conserved enzyme with moonlighting functions beyond glycolysis.
- Metal ion binding to GAPDH has been observed to inhibit its enzymatic activity, but the underlying mechanisms remain unclear.
Purpose of the Study:
- To investigate the effects of zinc, silver, and copper ions on Escherichia coli GAPDH (ecGAPDH) activity.
- To elucidate the mechanism of metal-induced inhibition of ecGAPDH.
Main Methods:
- Enzymatic activity assays under aerobic and anaerobic conditions.
- Electron paramagnetic spectroscopy.
- Mass spectrometry.
Main Results:
- Zinc ions (Zn2+) did not affect ecGAPDH activity.
- Copper ions (Cu2+) induced redox inactivation, with Cu+ binding tightly to the protein.
- Copper (Cu+) and silver (Ag+) ions sensitized ecGAPDH to oxidative inactivation by oxygen, a process that is reversible and involves modification of the active site cysteine.
Conclusions:
- Metal-induced oxidative modification of ecGAPDH acts as a reversible redox switch.
- This mechanism allows cells to redirect metabolic processes for protection against toxic metals and reactive oxygen species.
- The findings provide insight into cellular defense mechanisms involving sentinel enzymes.
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