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Cofactors and Coenzymes01:24

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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During the electron transport chain, electrons from NADH and FADH2 are first transferred to complexes I and II, respectively. These two complexes then transfer the electrons to ubiquinol, which carries them further to complex III. Complex III passes the electrons across the intermembrane space to Cyt c, which carries them further to complex IV. Complex IV donates electrons to oxygen and reduces it to water. As electrons pass through complexes I, III, and IV, the energy released aids the pumping...
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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
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Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
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Metallocofactor assembly for [FeFe]-hydrogenases.

Pedro Dinis1, Beata M Wieckowski1, Peter L Roach1

  • 1Chemistry and the Institute for Life Sciences, University of Southampton, Highfield Campus, Southampton SO17 1BJ, UK.

Current Opinion in Structural Biology
|June 27, 2016
PubMed
Summary
This summary is machine-generated.

Hydrogenases are key to bioenergy production. Researchers are uncovering how enzymes like HydG assemble the complex H-cluster cofactor, crucial for [FeFe]-hydrogenase function and hydrogen generation.

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Area of Science:

  • Biochemistry
  • Bioenergetics
  • Enzymology

Background:

  • Hydrogenases are vital enzymes for renewable energy, catalyzing hydrogen production using complex metallocofactors.
  • The [FeFe]-hydrogenase subclass relies on the intricate H-cluster cofactor, featuring a diiron subcluster linked to a [4Fe-4S] cluster.
  • Ligands for the diiron subcluster include azadithiolate, carbon monoxide, and cyanide, essential for catalytic activity.

Purpose of the Study:

  • To elucidate the biosynthesis pathway of the H-cluster cofactor in [FeFe]-hydrogenases.
  • To investigate the role of the maturase enzyme HydG in assembling the [2Fe]H subcluster precursor.
  • To understand the fragmentation mechanisms involved in diatomic ligand biosynthesis.

Main Methods:

  • Structural studies of enzyme-cofactor complexes.
  • Spectroscopic analysis to probe cofactor assembly.
  • Biochemical assays to characterize enzyme function.

Main Results:

  • Insights into the HydG-mediated assembly of the [2Fe]H subcluster precursor.
  • Characterization of the unusual fragmentation mechanism for diatomic ligand biosynthesis.
  • Understanding the initial steps of H-cluster cofactor assembly.

Conclusions:

  • The HydG enzyme plays a critical role in initiating the complex H-cluster biosynthesis pathway.
  • Structural and spectroscopic data provide a foundation for understanding hydrogenase cofactor maturation.
  • Further research into these mechanisms could advance biohydrogen production technologies.