Structural study of the X-ray-induced enzymatic reduction of molecular oxygen to water by Steccherinum murashkinskyi laccase: insights into the reaction mechanism

Acta Crystallogr D Struct Biol. 2017 May 1;73(Pt 5):388-401. doi: 10.1107/S2059798317003667. Epub 2017 Apr 26.


The laccase from Steccherinum murashkinskyi is a member of the large family of multicopper oxidases that catalyze the oxidation of a wide range of organic and inorganic substrates, accompanied by the reduction of dioxygen to water. The reducing properties of X-ray radiation and the high quality of the laccase crystals allow the study of the catalytic reduction of dioxygen to water directly in a crystal. A series of diffraction data sets with increasing absorbed radiation dose were collected from a single crystal of Steccherinum murashkinskyi laccase at 1.35 Å resolution. Changes in the active-site structure associated with the reduction of molecular oxygen to water on increasing the absorbed dose of ionizing radiation were detected. The structures in the series are mixtures of different states of the enzyme-substrate complex. Nevertheless, it was possible to interpret these structures as complexes of various oxygen ligands with copper ions in different oxidation states. The results allowed the mechanism of oxygen reduction catalyzed by laccases to be refined.

Keywords: enzymatic oxygen reduction; laccase; photo-electron reduction; reaction mechanisms; serial X-ray data.

MeSH terms

  • Biocatalysis / radiation effects
  • Catalytic Domain / radiation effects
  • Crystallography, X-Ray
  • Laccase / chemistry
  • Laccase / metabolism*
  • Models, Molecular
  • Oxidation-Reduction / radiation effects
  • Oxygen / metabolism*
  • Polyporales / chemistry
  • Polyporales / enzymology*
  • Polyporales / radiation effects
  • Protein Conformation / radiation effects
  • Water / metabolism*
  • X-Rays


  • Water
  • Laccase
  • Oxygen