Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase.
Ito, N., Phillips, S.E., Stevens, C., Ogel, Z.B., McPherson, M.J., Keen, J.N., Yadav, K.D., Knowles, P.F.(1991) Nature 350: 87-90
- PubMed: 2002850 
- DOI: https://doi.org/10.1038/350087a0
- Primary Citation of Related Structures:  
1GOF, 1GOG, 1GOH - PubMed Abstract: 
Galactose oxidase is an extracellular enzyme secreted by the fungus Dactylium dendroides. It is monomeric, with a relative molecular mass of 68,000, catalyses the stereospecific oxidation of a broad range of primary alcohol substrates and possesses a unique mononuclear copper site essential for catalysing a two-electron transfer reaction during the oxidation of primary alcohols to corresponding aldehydes. Recent evidence arguing against a Cu(III)-Cu(I) couple implies the existence of a second redox-active site proposed to involve pyrroloquinoline quinone or a tyrosine radical. We now report the crystal structure of galactose oxidase at 1.7 A resolution. This reveals a unique structural feature at the copper site with a novel thioether bond linking Cys 228 and Tyr 272 in a stacking interaction with Trp 290. We propose that these molecular components stabilize the protein free-radical species essential for catalysis and thus provide a 'built-in' secondary cofactor. This feature may represent a new mechanism for mediating electron transfer in metalloenzymes in the absence of exogenous cofactors.
Organizational Affiliation: 
Department of Biochemistry and Molecular Biology, University of Leeds, UK.