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Protein-radical enzymes

J Z Pedersen1, A Finazzi-Agrò

  • 1Department of Biology, Tor Vergata University of Rome, Italy.

FEBS Letters
|June 28, 1993
PubMed
Summary
This summary is machine-generated.

Protein-radical enzymes utilize intrinsic amino acid radicals as cofactors. These radicals act as one-electron gates, managing electron transfer in biological processes.

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Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Protein-radical enzymes are a class of enzymes that employ a radical cofactor.
  • This radical is derived from an intrinsic amino acid residue within the enzyme's active site.

Purpose of the Study:

  • To elucidate the mechanistic role of radical cofactors in protein-radical enzymes.
  • To categorize the types of amino acid residues involved in radical formation.

Main Methods:

  • Review of existing literature on protein-radical enzymes.
  • Analysis of amino acid residues known to form radicals in various enzyme families.

Main Results:

  • Identified tyrosine, modified tyrosine, tryptophan, modified tryptophan, and glycine as amino acids forming radical cofactors.

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  • Examples include ribonucleotide reductase, photosystem II, prostaglandin H synthase, amine oxidase, galactose oxidase, cytochrome c peroxidase, methylamine dehydrogenase, and pyruvate formate lyase.
  • The primary mechanistic role identified is that of a one-electron gate.
  • Conclusions:

    • Protein-radical enzymes utilize a diverse range of amino acid residues to generate radical cofactors.
    • These radical cofactors function as crucial one-electron gates, facilitating controlled electron transfer in enzymatic reactions.