Authentic and recombinant bilirubin oxidases are in different resting forms.
Myrothecium verrucaria bilirubin oxidase expressed in Aspergillus oryzae is in a resting form different from that of the authentic bilirubin oxidase, but reaches the resting form of the authentic enzyme after one cycle of reduction and reoxidation with dioxygen as shown by the absorption and electron paramagnetic resonance spectra.
Sakurai
Takeshi
T
Department of Chemistry, Faculty of Science, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan. ts0513@kenroku.kanazawa-u.ac.jp
Zhan
Lei
L
Fujita
Takahiro
T
Kataoka
Kunishige
K
Shimizu
Atsushi
A
Samejima
Tatsuya
T
Yamaguchi
Shotaro
S
D001203:Ascomycota / Q000201:enzymology; D001236:Aspergillus oryzae / Q000201:enzymology; D004578:Electron Spin Resonance Spectroscopy; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000235:genetics*; D010100:Oxygen / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry; D013056:Spectrophotometry, Ultraviolet
D011994:Recombinant Proteins; D044925:Oxidoreductases Acting on CH-CH Group Donors; C042401:bilirubin oxidase; D010100:Oxygen