Various enzymes, such as CYP56A1 and myeloperoxidase, catalyze the oxidation of tyrosine residues in protein chains to form dityrosine crosslinks in various organisms.

The 2,2′-biphenol structural motif allows dityrosine to form a complex with borate.

[3] Affinity chromatography with a column containing immobilised phenylboronic acid has allowed development of several methods for purification of dityrosine.

[4] The tyrosine–tyrosine crosslink can form by ultraviolet irradiation and other conditions that induce radical formation.

The monomer and dimer have different emission wavelengths, which can complicate fluorescence spectroscopic analysis of tyrosine-containing proteins.