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Related Concept Videos

Cofactors and Coenzymes01:27

Cofactors and Coenzymes

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Enzymes require additional components for proper function. There are two such classes of molecules: cofactors and coenzymes. Cofactors are metallic ions and coenzymes are non-protein organic molecules. Both of these types of helper molecule can be tightly bound to the enzyme or bound only when the substrate binds.
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Enzymes are proteins made of amino acids. The functional group of each constituent amino acid catalyzes a wide variety of chemical reactions via ionic interactions or acid-base reactions. However, amino acids cannot catalyze oxidation-reduction and group transfer reactions and need to be aided by non-protein components called cofactors. Cofactors are also referred to as the chemical teeth of an enzyme.
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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
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Updated: Apr 8, 2026

Immobilization of Multi-biocatalysts in Alginate Beads for Cofactor Regeneration and Improved Reusability
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Streamlined cofactor recycling with formate for chemo-enzymatic synthesis.

Di Jiang1, Xiangdong Xue1, Maoyuan Lv1

  • 1State Key Laboratory of Photoelectric Conversion and Utilization of Solar Energy, Qingdao New Energy Shandong Laboratory, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao 266101, P. R. China. xingfs@qibebt.ac.cn.

Chemical Communications (Cambridge, England)
|April 7, 2026
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Summary

A novel COF-OH-Rh catalyst efficiently regenerates NADH using formate via a hydrogen-radical pathway. This method minimizes byproducts and enhances L-glutamate synthesis when coupled with glutamate dehydrogenase.

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Area of Science:

  • Catalysis
  • Biocatalysis
  • Organic Chemistry

Background:

  • Nicotinamide adenine dinucleotide (NADH) is a crucial cofactor for numerous enzymatic reactions.
  • Efficient and sustainable NADH regeneration is essential for biocatalytic processes.
  • Current NADH regeneration methods often suffer from low efficiency or byproduct formation.

Purpose of the Study:

  • To develop a novel catalyst for formate-driven NADH regeneration.
  • To investigate the mechanism of NADH regeneration using a hydrogen-radical pathway.
  • To demonstrate the application of this system for high-yield L-glutamate synthesis.

Main Methods:

  • Synthesis and characterization of a COF-OH-Rh catalyst.
  • NADH regeneration assays using formate as the electron donor.
  • Spectroscopic and electrochemical studies to elucidate the reaction mechanism.
  • Coupling the NADH regeneration system with glutamate dehydrogenase for L-glutamate production.

Main Results:

  • The COF-OH-Rh catalyst demonstrated efficient NADH regeneration via a hydrogen-radical pathway.
  • This pathway minimized byproduct formation compared to traditional hydride transfer methods.
  • The coupled system achieved high-yield L-glutamate synthesis, showcasing practical applicability.

Conclusions:

  • COF-OH-Rh serves as an effective catalyst for formate-driven NADH regeneration.
  • The hydrogen-radical pathway offers a promising alternative for sustainable biocatalysis.
  • This approach facilitates efficient production of valuable biochemicals like L-glutamate.