Compensatory binding of an asparagine residue to the coordination-unsaturated type I Cu center in bilirubin oxidase mutants.
Met467, the axial ligand to type I Cu in a multicopper oxidase, Myrothecium verrucaria bilirubin oxidase was substituted with a non-coordinating Phe and Leu to transform the spectral and magnetic properties and oxidase activities of the enzyme into those of fungal laccases, but the mutated type I Cu center showed properties characteristic of phytocyanins, blue copper proteins with an axial coordination of Gln, due to compensatory binding of the distal Asn459 as evidenced by a double mutation.
Kataoka
Kunishige
K
Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan.
Tsukamoto
Keishi
K
Kitagawa
Rieko
R
Ito
Takahiro
T
Sakurai
Takeshi
T
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D001216:Asparagine / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites / Q000235:genetics; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics; D003300:Copper / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics; D006999:Hypocreales / Q000201:enzymology*; D008969:Molecular Sequence Data; D009154:Mutation; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000235:genetics
D002352:Carrier Proteins; D005656:Fungal Proteins; C023548:copper-binding protein; D001216:Asparagine; D003300:Copper; D044925:Oxidoreductases Acting on CH-CH Group Donors; C042401:bilirubin oxidase