concept

Topaquinone (TPQ)

The structure of a new biological redox cofactor-topaquinone (TPQ), the quinone of 2,4,5-trihydroxyphenylalanine-was elucidated in 1990. TPQ is the cofactor in most copper-containing amine oxidases. It is produced by post-translational modification of a strictly conserved active-site tyrosine residue. Recent work has established that TPQ biogenesis proceeds via a novel self-processing pathway requiring only the protein, copper, and molecular oxygen. The oxidation of tyrosine to TPQ by dioxygen is a six-electron process, which has intriguing mechanistic implications because copper is a one-electron redox agent, and dioxygen can function as either a two-electron or four-electron oxidant.

Ref:
Dooley DM. Structure and biogenesis of topaquinone and related cofactors. J Biol Inorg Chem. 1999 Feb;4(1):1-11. doi: 10.1007/s007750050283. PMID: 10499097.

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Added on Dec 11, 2023 by Barbara Van De Keer

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