A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes

Leena Penttinen, Chiara Rutanen, Markku Saloheimo, Kristiina Kruus, Juha Rouvinen, Nina Hakulinen

Research output: Contribution to journalArticleScientificpeer-review

1 Citation (Scopus)

Abstract

Coupled binuclear copper (CBC) enzymes have a conserved type 3 copper site that binds molecular oxygen to oxidize various mono- and diphenolic compounds. In this study, we found a new crystal form of catechol oxidase from Aspergillus oryzae (AoCO4) and solved two new structures from two different crystals at 1.8-Å and at 2.5-Å resolutions. These structures showed different copper site forms (met/deoxy and deoxy) and also differed from the copper site observed in the previously solved structure of AoCO4. We also analysed the electron density maps of all of the 56 CBC enzyme structures available in the protein data bank (PDB) and found that many of the published structures have vague copper sites. Some of the copper sites were then re-refined to find a better fit to the observed electron density. General problems in the refinement of metalloproteins and metal centres are discussed.

Original languageEnglish
Article numbere0196691
JournalPLoS ONE
Volume13
Issue number5
DOIs
Publication statusPublished - 1 May 2018
MoE publication typeA1 Journal article-refereed

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Aspergillus oryzae
Catechol Oxidase
Aspergillus
catechol oxidase
crystals
Copper
copper
Crystals
Enzymes
enzymes
Carrier concentration
metalloproteins
electrons
Metalloproteins
Electrons
Molecular oxygen
Metals
metals
Databases
Oxygen

Cite this

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A new crystal form of Aspergillus oryzae catechol oxidase and evaluation of copper site structures in coupled binuclear copper enzymes. / Penttinen, Leena; Rutanen, Chiara; Saloheimo, Markku; Kruus, Kristiina; Rouvinen, Juha; Hakulinen, Nina.

In: PLoS ONE, Vol. 13, No. 5, e0196691, 01.05.2018.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Hakulinen, Nina

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