The crystal structure of an extracellular catechol oxidase from the ascomycete fungus Aspergillus oryzae

Nina Hakulinen*, Chiara Gasparetti, Heidi Kaljunen, Kristiina Kruus, Juha Rouvinen

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

29 Citations (Scopus)

Abstract

Catechol oxidases (EC 1.10.3.1) catalyse the oxidation of o-diphenols to their corresponding o-quinones. These oxidases contain two copper ions (CuA and CuB) within the so-called coupled type 3 copper site as found in tyrosinases (EC 1.14.18.1) and haemocyanins. The crystal structures of a limited number of bacterial and fungal tyrosinases and plant catechol oxidases have been solved. In this study, we present the first crystal structure of a fungal catechol oxidase from Aspergillus oryzae (AoCO4) at 2.5-Å resolution. AoCO4 belongs to the newly discovered family of short-tyrosinases, which are distinct from other tyrosinases and catechol oxidases because of their lack of the conserved C-terminal domain and differences in the histidine pattern for CuA. The sequence identity of AoCO4 with other structurally known enzymes is low (less than 30 %), and the crystal structure of AoCO4 diverges from that of enzymes belonging to the conventional tyrosinase family in several ways, particularly around the central α-helical core region. A diatomic oxygen moiety was identified as a bridging molecule between the two copper ions CuA and CuB separated by a distance of 4.2-4.3 Å . The UV/vis absorption spectrum of AoCO4 exhibits a distinct maximum of absorbance at 350 nm, which has been reported to be typical of the oxy form of type 3 copper enzymes.

Original languageEnglish
Pages (from-to)917-929
Number of pages13
JournalJOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume18
Issue number8
DOIs
Publication statusPublished - 17 Sep 2013
MoE publication typeA1 Journal article-refereed

Keywords

  • Binuclear copper site
  • Catechol oxidase
  • Type 3 copper enzymes
  • Tyrosinase
  • X-ray crystallography

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