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Cofactors and Coenzymes

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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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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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Related Experiment Video

Updated: Mar 26, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Waltzing around cofactors.

Percival Yang-Ting Chen¹, Elizabeth C Wittenborn¹, Catherine L Drennan²

¹Department of Chemistry, Massachusetts Institute of Technology, Cambridge, United States.

|February 5, 2016

Summary

This summary is machine-generated.

The nitrogenase metallocofactor, crucial for nitrogen fixation, is more flexible than previously believed. This finding impacts our understanding of this essential biological process.

Keywords:

Azotobacter vinelandii biochemistry biophysics iron sulfur proteins metalloproteins nitrogen fixation structural biology

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Area of Science:

Biochemistry
Molecular Biology
Enzyme Catalysis

Background:

Nitrogen fixation is a vital process for life, converting atmospheric nitrogen into ammonia.
The metallocofactor of nitrogenase enzymes is central to this conversion.
Previous models depicted this metallocofactor as a rigid structure.

Purpose of the Study:

To investigate the structural dynamics of the nitrogenase metallocofactor.
To challenge the prevailing notion of a rigid metallocofactor scaffold.

Main Methods:

Utilizing advanced spectroscopic techniques to probe the metallocofactor's environment.
Employing computational modeling to simulate cofactor behavior under reaction conditions.

Main Results:

The metallocofactor exhibits significant conformational flexibility.
Evidence suggests dynamic structural changes during the catalytic cycle.
The scaffold is not rigid, contrary to prior assumptions.

Conclusions:

The nitrogenase metallocofactor is a dynamic entity, not a static scaffold.
This flexibility is likely essential for the enzyme's catalytic efficiency.
Revising structural models is necessary for a complete understanding of nitrogen fixation.