Related Experiment Video
Updated: May 31, 2026
11:16
Hydrophobic Salt-modified Nafion for Enzyme Immobilization and Stabilization
Published on: July 11, 2012
Chemically engineered papain as artificial formate dehydrogenase for NAD(P)H regeneration
Pierre Haquette1, Barisa Talbi, Laure Barilleau
1Chimie ParisTech, Laboratoire Charles Friedel, Paris, France.
Organic & Biomolecular Chemistry
|June 23, 2011
Summary
Rh(III) and Ru(II) organometallic complexes catalyze the reduction of enzyme cofactors NAD(P)(+) to NAD(P)H. Rh(III) complexes showed higher potency, and hybrid metalloproteins exhibited formate dehydrogenase activity.
Area of Science:
- Organometallic Chemistry
- Biocatalysis
- Enzyme Engineering
Background:
- Organometallic complexes are explored for catalytic applications.
- Enzyme cofactors like NAD(P)(+) require efficient reduction methods.
- Developing novel catalysts for NAD(P)H regeneration is crucial for biochemical processes.
Purpose of the Study:
- To synthesize and evaluate organometallic complexes as catalysts for NAD(P)(+) reduction.
- To compare the catalytic activity of Rh(III) and Ru(II) complexes.
- To investigate the formation and activity of hybrid metalloproteins.
Main Methods:
- Synthesis of Ru(II) and Rh(III) complexes with various ligands (N⁁N, arene).
- Catalytic reduction of NAD(P)(+) using formate as a hydride donor.
- Covalent immobilization of complexes onto papain enzyme.
Main Results:
- Identified Ru(II) and Rh(III) complexes as catalysts for stereoselective NAD(P)(+) reduction.
- Rh(III) complexes demonstrated significantly higher catalytic potency (TOF) than Ru(II) complexes.
- Covalently anchored hybrid metalloproteins displayed formate dehydrogenase activity.
Conclusions:
- The choice of ligands (N⁁N and arene) influences the activity of Ru(II) catalysts.
- Rh(III) complexes are superior catalysts for NAD(P)(+) reduction compared to Ru(II) counterparts.
- Hybrid metalloproteins offer a promising platform for biocatalytic applications with tunable activity.
