@article{oai:kanazawa-u.repo.nii.ac.jp:00010831,
 author = {Kajikawa, Takao and Sugiyama, Ryosuke and Kataoka, Kunishige and Sakurai, Takeshi},
 journal = {Journal of Inorganic Biochemistry},
 month = {Aug},
 note = {A multicopper oxidase, CueO was doubly mutated at its type I copper ligand, Cys500 and an acidic amino acid residue located in the proton transfer pathway, Glu506, to Ser and Ala, respectively. Cys500Ser/Glu506Ala was mainly in a novel resting form to afford the absorption band at ca. 400. nm and an EPR signal with a highly anisotropic character derived from type III copper. However, Cys500Ser/Glu506Ala gave the same reaction intermediate (peroxide intermediate) as that from Cys500Ser and Cys500Ser/Glu506Gln. © 2015 Elsevier Inc., Embargo Period 24 months},
 pages = {88--90},
 title = {A novel resting form of the trinuclear copper center in the double mutant of a multicopper oxidase, CueO, Cys500Ser/Glu506Ala},
 volume = {149},
 year = {2015}
}