Redox potentials of the blue copper sites of bilirubin oxidases.
The redox potentials of the multicopper redox enzyme bilirubin oxidase (BOD) from two organisms were determined by mediated and direct spectroelectrochemistry. The potential of the T1 site of BOD from the fungus Myrothecium verrucaria was close to 670 mV, whereas that from Trachyderma tsunodae was >650 mV vs. NHE. For the first time, direct electron transfer was observed between gold electrodes and BODs. The redox potentials of the T2 sites of both BODs were near 390 mV vs. NHE, consistent with previous finding for laccase and suggesting that the redox potentials of the T2 copper sites of most blue multicopper oxidases are similar, about 400 mV.
Christenson
Andreas
A
Department of Analytical Chemistry, Lund University, P.O. Box 124, SE-221 00 Lund, Sweden.
Shleev
Sergey
S
Mano
Nicolas
N
Heller
Adam
A
Gorton
Lo
L
D000595:Amino Acid Sequence; D020134:Catalytic Domain / Q000235:genetics; D003300:Copper / Q000737:chemistry*; D004579:Electron Transport; D032902:Ganoderma / Q000201:enzymology / Q000235:genetics; D006999:Hypocreales / Q000201:enzymology / Q000235:genetics; D008564:Membrane Potentials; D010084:Oxidation-Reduction; D044925:Oxidoreductases Acting on CH-CH Group Donors / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D003300:Copper; D044925:Oxidoreductases Acting on CH-CH Group Donors; C042401:bilirubin oxidase