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Protein oxidation involved in Cys-Tyr post-translational modification.

Susan E Hromada1, Adam M Hilbrands1, Elysa M Wolf1

  • 1Department of Chemistry & Biochemistry, Calvin College, Grand Rapids, MI 49546, United States.

Journal of Inorganic Biochemistry
|September 18, 2017
PubMed
Summary
This summary is machine-generated.

Post-translational modification creates unique redox-active tyrosines (Cys-Tyr) in proteins. This study reveals surface tyrosine oxidation as a side reaction during Cys-Tyr cofactor formation in BF4112.

Keywords:
Copper-dioxygen activationCys-TyrNative fluorescenceOuter sphere electron transferProtein-derived cofactorsSurface tyrosine oxidation

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Area of Science:

  • Biochemistry
  • Protein Chemistry
  • Redox Biology

Background:

  • Post-translational modifications of tyrosine residues can create unique redox-active cofactors.
  • The intramolecular thioether-crosslinked 3'-(S-cysteinyl)-tyrosine (Cys-Tyr) is a well-studied modification found in enzymes like galactose oxidase.
  • Cys-Tyr linkages are also present in mammalian cysteine dioxygenases and have been observed in orphan proteins like BF4112.

Purpose of the Study:

  • To investigate the formation of Cys-Tyr in the orphan protein BF4112.
  • To characterize the role of metal ions and specific residues in Cys-Tyr formation.
  • To explore potential side reactions and their impact on cofactor synthesis.

Main Methods:

  • UV-Vis spectroscopy for characterization of protein modifications.
  • Fluorescence-based assays for quantifying Cys-Tyr yield, with guanidinium chloride for specificity.
  • Site-directed mutagenesis to replace key tyrosine and cysteine residues.
  • Denaturing SDS-PAGE to analyze protein products.

Main Results:

  • Cys-Tyr formation in BF4112 was dependent on the presence of Tyr 52, Cys 98, and a Cu2+ ion.
  • Mutations to Tyr 52 (to Phe) or Cu2+ (to Zn2+) abolished Cys-Tyr formation.
  • Mutations to surface tyrosines and Cys 98 reduced Cys-Tyr yield but revealed a red-shifted emission, indicating surface tyrosyl radical (dityrosine) formation when Cys 98 was replaced by Ser.

Conclusions:

  • Protein oxidation, specifically surface tyrosine oxidation, is a significant side reaction during Cys-Tyr cofactor formation in BF4112.
  • The study highlights the complexity of post-translational cofactor synthesis and potential competing reaction pathways.
  • Understanding these side reactions is crucial for accurately characterizing protein-derived cofactors and their biological roles.