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(4E,15Z)-cyclobilirubin IX alpha + O2
?
-
phosphate buffer, pH 3.5-7.4
-
-
?
(4Z,15E)-bilirubin IX alpha + O2
?
-
no activity above pH 4.5 in phosphate buffer
-
-
?
(4Z,15Z)-bilirubin IX alpha + O2
?
-
no activity above pH 5.5 in phosphate buffer, no acticvity in citrate-lactate buffer, pH 3.7
-
-
?
1,1'-dimethylferrocene + O2
1,1'-dimethylferricenium + H2O
-
1,1'-dimethylferrocene soluble as an inclusion complex with 2-hydroxypropyl-beta-cyclodextrin
-
?
1,3-dihydroxynaphthalene + O2
?
-
-
-
-
?
1,5-dihydroxynaphthalene + O2
?
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
2 bilirubin + O2
2 biliverdin + H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
?
2,2'-azino-di-[3-ethylbenzthiazoline-6-sulfonic acid] + O2
?
2,6-dimethoxyphenol + O2
? + H2O
bilirubin + O2
biliverdin + H2O
bilirubin ditaurine + O2
?
-
-
-
-
?
catechol + O2
?
-
67% of activity with bilirubin
-
-
?
chlorophyllin + O2
?
-
50% of activity with bilirubin
-
-
?
cytochrome c + O2
?
-
BOD efficiently accepts cytochrome c as an electron donor in both cases when cytochrome c is in solution or electrostatically adsorbed
-
-
?
Fe(CN)64- + O2
Fe(CN)63- + H2O
-
-
-
-
?
ferricyanide + O2
? + H2O
-
-
-
?
ferrocene + O2
ferricinium + H2O
-
low activity
-
?
ferrocyanide + O2
?
-
-
-
-
?
ferrocyanide + O2
ferricyanide + H2O
hemin + O2
?
-
10% of activity with bilirubin
-
-
?
hexacyanoferrate(II) + O2
hexacyanoferrate(III) + H2O
-
-
-
-
?
hydroquinone + O2
?
-
20% of activity with bilirubin
-
-
?
indigo carmine + O2
?
-
dye decolorization reaction
-
-
?
K4[Fe(CN)6] + O2
K3[Fe(CN)6] + H2O
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
octacyanotungstate(IV) + O2
octacyanotungstate(V) + H2O
-
-
-
-
?
p-phenylenediamine + O2
?
phenol 2,6-dimethoxyphenol + O2
?
pyrogallol + O2
?
-
10% of activity with bilirubin
-
-
?
Remazol Brilliant Blue + O2
?
Remazol Brilliant Blue R + O2
?
syringaldazine + O2
?
-
-
-
-
?
syringaldazine + O2
oxidized syringaldazine + H2O
[Fe(CN)6]4- + H+ + O2
[Fe(CN)6]3- + H2O
-
-
-
-
?
additional information
?
-
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
the enzyme from Bacillus pumilus shows higher turnover activity towards bilirubin compared to other bacterial MCOs
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
substrates are unconjugated bilirubin and conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
substrate conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + 2 H2O
-
substrate conjugated bilirubin
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
?
2 bilirubin + O2
2 biliverdin + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
i.e. ABTS
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
the enzyme has a higher affinity for oxygen in the presence of the nanoparticles compared to the dissolved 2,2`-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) mediator, although with a slower turnover rate
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
BOD encapsulated in ananostructured sol-gel/carbon nanotube composite electrode effectively catalyzes the reduction of molecular oxygen into water through direct electron transfer
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
? + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + H2O
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonate) + O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzthiazoline-6-sulfonic acid] + O2
?
-
-
-
-
?
2,2'-azino-di-[3-ethylbenzthiazoline-6-sulfonic acid] + O2
?
-
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
?
2,6-dimethoxyphenol + O2
? + H2O
-
-
-
?
ascorbic acid + O2
?
-
very low activity
-
-
?
ascorbic acid + O2
?
-
very low activity
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
655037, 655920, 657282, 672031, 684405, 684426, 684921, 685430, 686068, 686371, 686377, 688004 -
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
r
bilirubin + O2
biliverdin + H2O
-
-
no formation of H2O2
?
bilirubin + O2
biliverdin + H2O
-
enzyme also exhibits laccase activity
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
CotA with markedly higher affinity for bilirubin than conventional bilirubin oxidase
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
-
r
bilirubin + O2
biliverdin + H2O
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
bilirubin + O2
biliverdin + H2O
-
-
biliverdin + colourless diazo-negative compounds, including propentdyopents
?
bilirubin + O2
biliverdin + H2O
-
-
biliverdin + colourless diazo-negative compounds, including propentdyopents
?
bilirubin + O2
biliverdin + H2O
-
-
-
?
biliverdin + O2
?
-
-
-
-
?
biliverdin + O2
?
-
50% of activity with bilirubin
-
-
?
Congo Red + O2
?
100% decoloration efficiency is reached for Congo Red at pH 4.0 in 8 h
-
-
?
Congo Red + O2
?
100% decoloration efficiency is reached for Congo Red at pH 4.0 in 8 h
-
-
?
ditaurobilirubin + O2
?
-
-
-
-
?
ditaurobilirubin + O2
?
-
-
-
-
?
ferrocyanide + O2
ferricyanide + H2O
-
-
-
?
ferrocyanide + O2
ferricyanide + H2O
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
-
-
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
-
23% of activity with bilirubin
-
-
?
N,N-dimethyl-p-phenylenediamine + O2
?
-
-
-
-
?
o-aminophenol + O2
?
-
-
-
-
?
o-aminophenol + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
p-phenylenediamine + O2
?
-
15% of activity with bilirubin
-
-
?
p-phenylenediamine + O2
?
-
-
-
-
?
phenol 2,6-dimethoxyphenol + O2
?
-
-
-
?
phenol 2,6-dimethoxyphenol + O2
?
-
-
-
?
Remazol Brilliant Blue + O2
?
80% decoloration efficiency is reached for Remazol Brilliant Blue at pH 8.2 in 24 h
-
-
?
Remazol Brilliant Blue + O2
?
80% decoloration efficiency is reached for Remazol Brilliant Blue at pH 8.2 in 24 h
-
-
?
Remazol Brilliant Blue R + O2
?
-
decolorization reaction
-
-
?
Remazol Brilliant Blue R + O2
?
-
decolorization reaction
-
-
?
syringaldazine + O2
oxidized syringaldazine + H2O
-
-
-
?
syringaldazine + O2
oxidized syringaldazine + H2O
-
-
-
?
additional information
?
-
-
cytochrome c and bilirubin oxidase are coimmobilized in a polyelectrolyte multilayer on gold electrodes and although these two proteins are not natural reaction partners, the protein architecture facilitates an electron transfer from the electrode through multiple protein layers to molecular oxygen
-
-
?
additional information
?
-
-
activity measurement with Fe(CN)6 4-
-
-
?
additional information
?
-
-
decolorization and biodegradation of remazol brilliant blue R, an anthraquinone dye, by bilirubin oxidase
-
-
?
additional information
?
-
direct proton uptake of Glu463 plays a key role in the proton donation to the activated oxygen species in the catalytic cycle, redox-induced protonation state changes of Glu463, electrochemistry-induced ATR-FTIR spectroscopy, overview
-
-
?
additional information
?
-
-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26°C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30°C to 50°C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml, overview
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
the enzyme is also active with the laccase substrate 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate)
-
-
?
additional information
?
-
oxidative polymerization of dihydroquercetin from Larix sibirica using bilirubin oxidase as a biocatalyst. DHQ oligomers (oligoDHQ) with molecular mass of 2800 and polydispersity of 8.6 are obtained by enzymatic reaction under optimal conditions. The oligomers appear to be soluble in dimethylsulfoxide, dimethylformamide, and methanol. UVvisible spectra of oligoDHQ in dimethylsulfoxide indicate the presence of highly conjugated bonds. Irregular structure of a polymer formed via the enzymatic oxidation of DHQ followed by nonselective radical polymerization. As compared with the monomer, oligoDHQ demonstrates higher thermal stability and high antioxidant activity
-
-
?
additional information
?
-
the enzyme needs to be fully reduced before it gets activated for catalysis
-
-
?
additional information
?
-
-
the enzyme needs to be fully reduced before it gets activated for catalysis
-
-
?
additional information
?
-
-
the oxygen reduction reaction activity of the enzyme with direct electron transfer reactions is higher than that with mediated electron transfer reactions
-
-
-
additional information
?
-
-
extracellular bilirubin oxidase decolorizes indigo carmine, biosorption and biodegradation of the dye is achved with more than 98% decolorization efficiency after 7 days at 26°C. Additionally, the crude bilirubin oxidase can efficiently decolorize indigo carmine at 30°C to 50°C and pH 5.5-9.5 with dye concentrations of 50-200 mg/ml, overview
-
-
?
additional information
?
-
-
the enzyme is also active with the laccase substrate 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate)
-
-
?
additional information
?
-
-
decolorization and biodegradation of remazol brilliant blue R, an anthraquinone dye, by bilirubin oxidase
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
the enzyme is also activity with the laccase, EC 1.10.3.2, substrates 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine and 2,6-dimethoxyphenol
-
-
?
additional information
?
-
usage of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol as substrates, optimization of the assay method
-
-
?
additional information
?
-
-
usage of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol as substrates, optimization of the assay method
-
-
?
additional information
?
-
usage of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,6-dimethoxyphenol as substrates, optimization of the assay method
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
O2 is catalytically reduced on BOD-modified spectrographic graphite electrodes, very slow direct electron transfer is observed for the enzyme absorbed on gold electrodes
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
in addition to traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate), syringaldazine, or 2,6-dimethoxyphenol, the enzyme catalyzes also the oxidation of conjugated and/or unconjugated bilirubin
-
-
?
additional information
?
-
-
in addition to the oxidation of bilirubin to biliverdin and of biliverdin to a purple pigment, BODs utilize also the more traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate) and syringaldazine. The enzyme is efficient in decolorizing textile dyes such as Remazol brilliant Blue R
-
-
?
additional information
?
-
-
in addition to the oxidation of bilirubin to biliverdin and of biliverdin to a purple pigment, BODs utilize also the more traditional laccase substrates like 2, 2'-azino-bis (3-ethylbenzthiazoline-6-sulfonate) and syringaldazine. The enzyme is efficient in decolorizing textile dyes such as Remazol brilliant Blue R
-
-
?
additional information
?
-
in the presence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as the mediator, the enzyme decolorizes crystal violet, malachite green and Congo red dyes at a rate of about 36%, 63% and 71%, respectively in 2 h
-
-
-
additional information
?
-
in the presence of 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as the mediator, the enzyme decolorizes crystal violet, malachite green and Congo red dyes at a rate of about 36%, 63% and 71%, respectively in 2 h
-
-
-
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0.00041
-
mutant enzyme M467L, using bilirubin as a substrate
0.00047
-
mutant enzyme N459A/M467F, using bilirubin as a substrate
0.00051
-
enzyme activity in small intestine
0.00064
-
mutant enzyme M467F, using bilirubin as a substrate
0.00157
-
enzyme activity in liver mitochondria
0.074
-
M467G mutant enzyme
0.3
-
ferrocyanide oxidase activity of mutant M467G
1.19
-
mutant enzyme M467Q, using bilirubin as a substrate
1.2
-
bilirubin oxidase activity of mutant D105A
11
-
bilirubin oxidase activity of mutant D105E
15.45
-
purified wild type enzyme, at pH 7.0 and 37°C
214.3
-
purified enzyme after anion exchange chromatography step, pH 7.5, 25°C
25.4
-
purified enzyme with substrate 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), pH 6.0, 24°C
46.1
-
recombinant wild type enzyme, using bilirubin as a substrate
8.03
-
enzyme immobilized on alginate-silicate beads
2.83
-
-
2.83
-
commercial preparation, pH not specified in the publication, temperature not specified in the publication
24
-
recombinant wild-type enzyme expressed in Aspergillus oryzae
24
-
bilirubin oxidase activity of authentic enzyme
24
-
bilirubin oxidase activity of recombinant enzyme
additional information
-
3.3 units/ml, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
-
206 units/A280, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
-
0.0013 mmol O2/min/0.08 mg protein
additional information
-
no bilirubin oxidase activity of mutant C457S and mutant D105N
additional information
-
relative activity 0.09, 0.2 g/l BOD stored in 0.5 g/l poly[ethyleneimine], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.09, 0.2 g/l BOD stored in 2 g/l poly[ethyleneimine], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.17, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M H2PO4--HPO42- buffer system, no additive
additional information
-
relative activity 0.17, 0.2 g/l BOD stored in 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.19, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M MOPS0-MOPS- buffer system, no additive
additional information
-
relative activity 0.22, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,6-hexanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.22, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.22, 0.2 g/l BOD stored in 2 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,6-hexanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.22, 0.2 g/l BOD stored in 2 g/l poly[(dimethylimino)-1,6-hexanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.23, 0.2 g/l BOD stored in 0.5 g/l poly(diallydimethylammonium), 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.23, 0.2 g/l BOD stored in 2 g/l poly(diallydimethylammonium), 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.25, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene]
additional information
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relative activity 0.26, 0.2 g/l BOD stored in 0.5 g/l poly[metacrylpropyltrimethylammonium], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.26, 0.2 g/l BOD stored in 2 g/l poly[metacrylpropyltrimethylammonium], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.27, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)-(dimethylimino)-1,3-propanediyl]
additional information
-
relative activity 0.27, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea]
additional information
-
relative activity 0.27, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.27, 0.2 g/l BOD stored in 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.28, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M H2PO4--HPO42- buffer system, 0.5 g/l poly(dimethylamine-co-epichrohydrin)
additional information
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relative activity 0.28, 0.2 g/l BOD stored in 0.5 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M H2PO4--HPO42- buffer system, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.28, 0.2 g/l BOD stored in 0.5 g/l poly[allyamine], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.28, 0.2 g/l BOD stored in 2 g/l poly[allyamine], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.30, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea]
additional information
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relative activity 0.30, 0.2 g/l BOD stored in 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.30, 0.2 g/l BOD stored in 2 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.31, 0.2 g/l BOD stored in 0.5 g/l poly[lysine], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.31, 0.2 g/l BOD stored in 2 g/l poly[lysine], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.38, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly(dimethylamine-co-epichrohydrin)
additional information
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relative activity 0.38, 0.2 g/l BOD stored in 0.5 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.38, 0.2 g/l BOD stored in 2 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.40, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene]
additional information
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relative activity 0.43, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M MOPS0-MOPS- buffer system, 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-etanediyl)-(dimethylimino)-1,3-propanediyl]
additional information
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relative activity 0.43, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.43, 0.2 g/l BOD stored in 2 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M MOPS-NaOH solution, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.51, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, no additive
additional information
-
relative activity 0.51, 0.2 g/l BOD stored in 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.58, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-etanediyl)-(dimethylimino)-1,3-propanediyl]
additional information
-
relative activity 0.58, 0.2 g/l BOD stored in 0.5 g/l poly[(dimethylimino)(2-oxo-1,2-ethanediyl)imino-1,2-ethanediylimino(1-oxo-1,2-ethanediyl)(dimethylimino)-1,3-propanediyl], 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30°C, 2 days
additional information
-
relative activity 0.64, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea]
additional information
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relative activity 0.64, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly[oxyethylene(dimethylimino)propyl(dimethylimino)ethylene]
additional information
-
relative activity 0.64, 0.2 g/l BOD stored in 0.5 g/l poly[bis(2-chloroethyl)ether-alt-1,3-bis[3-(dimethylimino)propyl]urea], 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30°C, 2 days
additional information
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relative activity 0.89, 0.2 g/l BOD stored at 30°C for 2 days in 0.1 M BisTrisH+-BisTris0 buffer system, 0.5 g/l poly(dimethylamine-co-epichrohydrin)
additional information
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relative activity 0.89, 0.2 g/l BOD stored in 0.5 g/l poly(dimethylamine-co-epichrohydrin), 0.1 M BisTrisH+-BisTris0 buffer system, pH 7.0, 30°C, 2 days
additional information
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mutant C457S shows no activity
additional information
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0.67 units/ml, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
additional information
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0.02 units/ml, 1 unit is defined as the equivalent amount of enzyme that reduces DELTA A at 440 nm by 1.05/min, enzyme activity in crude extracts
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biotechnology
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bilirubin oxidase has been found to be the best enzyme for converting O2 to H2O as a cathodic enzyme in biofuel cells
C457A
-
no oxidase activity
C457S
-
can react with dioxygen, affords reaction intermediate I with absorption maxima at 340, 470, and 675 nm
C457V
-
no oxidase activity
D105A
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exhibits 7.5% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II
D105E
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exhibits 46% bilirubin oxidase activity compared to the wild-type enzyme, indicating that Asp105 conserved in all multi-copper oxidases donates a proton to reaction intermediates I and II
D105N
-
does not react with dioxygen
E463Q
site-directed mutagenesis
H134/136V
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no oxidase activity
H456/458V
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no oxidase activity
H456D/H458D
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mutant with weak bilirubin oxidase and ferroxidase activity
H456K/H458K
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mutant with weak bilirubin oxidase and ferroxidase activity
H456V/H458V
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inactive mutant
H94V
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no oxidase activity
M467F
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the mutated type I Cu center shows characteristics of phytocyanins
M467L
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the mutated type I Cu center shows characteristics of phytocyanins
Met467Q
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reduced activity
N394A/W396T
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the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected
N459A/M467F
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activity is decreased to 1% of the recombinant wild type enzyme, the mutated type I Cu center shows characteristics of phytocyanins, blue copper proteins with an axial coordination of Gln, due to compensatory binding of the distal Asn459
W396D
the mutant shows practically zero activity compared to the wild type enzyme
W396T
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the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected
W396Y
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the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected
W396A
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the mutant shows increased activity with bilirubin, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) or ferricyanide compared to the wild type enzyme
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W396D
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the mutant shows practically zero activity compared to the wild type enzyme
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W396F
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the mutant shows decreased activity with bilirubin and increased activity with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) or ferricyanide compared to the wild type enzyme
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C457S
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virtually no enzyme activity, Ru-incorporation conferrs higher enzyme activity
I402G
-
low enzyme activity
M467G
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weak oxidase activity
M467G
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with modified spectroscopic properties and redox potential, affords reaction intermediate II with absorption maxima at 355 and 450 nm
M467Q
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the enzymatic activity of the mutant is very low toward bilirubin but it works as a good catalyst in direct electron transfer-type bioelectrocatalytic reduction of dioxygen into water, the kcat value is 3fold increased
M467Q
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the catalytic activity of the mutant is quite low (about 0.3% of wild type activity)
M467Q
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the mutant is inactive against bilirubin. A post-translational crosslink between Trp396 and His398, formed in the vicinity of the T1Cu site in wild type enzyme, is absent in the mutant
W396A
-
the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected
W396A
the mutant shows increased activity with bilirubin, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) or ferricyanide compared to the wild type enzyme
W396F
-
the enzymatic activity of the mutant is prominently decreased compared to the wild type enzyme. The enzyme shows shifts in the redox potential of type I copper towards negative direction by more than 100 mV and decreases in cathodic current in electrochemistry, whereas optical and magnetic properties of type I copper are not affected or sparingly affected
W396F
the mutant shows decreased activity with bilirubin and increased activity with 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) or ferricyanide compared to the wild type enzyme
additional information
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attachment of the purified enzyme to a PGE surface, from pyrolytic graphite plates, modified with 6-amino-2-naphthoic acid, modifiers tested in increasing activity are 4-aminothiophenol, 4-aminobenzonitrile, 2-aminoacridine, 2-aminoanthracene, 1-aminoanthracene, 2-aminochrysene, 4-benzyloxyaniline, 4-aminobenzoic acid, 4-aminophenylacetic acid, 6-amino-2-naphthoic acid, the latter giving best results. Method optimization, cyclic voltammetry measuring the electrocatalytic reduction of dioxygen by platinum electrodeposited on PGE, detailed overview
additional information
enzyme immobilization and preparation of a bilirubin oxidase-based air breathing cathode, evaluation by constant monitoring over 45 days, analysis of effect of electrolyte composition on the cathode oxygen reduction reaction output, and of deactivation of the electrocatalytic activity of the enzyme in phosphate buffer saline solution and in activated sludge, anions and cations in autoclaved activated sludge with PBS, overview. Enzyme deactivation is also studied in activated sludge to simulate an environment close to the real waste operation with pollutants, solid particles and bacteria. The presence of low-molecularweight soluble contaminants is identified as the main reason for an immediate enzymatic deactivation within few hours of cathode operation. The presence of solid particles and bacteria does not affect the natural degradation of the enzyme
additional information
enzyme immobilization on an electrode, bilirubin oxidase adsorbed on a nanocomposite modified electrode has three distinct redox sites within that show pH dependence: the 1st redox centre with the highest redox potential Ec(1st) = 404 mV vs. Ag/AgCl (614 mV vs. NHE at pH 7.0) exhibits pH dependence with a slope -dEc(1st)/dpH = 66 mVunder a non-turnover process. The 2nd redox centre with a potential Ec(2nd) = 228 mV vs. Ag/AgCl (438 mV vs. NHE at pH 7.0) is not dependent on pH in the absence and presence of O2. Finally, the 3rd redox site with a redox potential Ec(3rd) = 92 mVvs. Ag/AgCl (302 mV vs. NHE at pH 7.0) exhibits pH dependence for a cathodic process with -dEc(3rd)/dpH = 70 mV and for anodic process with -dEa(3rd)/dpH = 73 mV, respectively. Two break points for dependence of Ec(1st) or Ec(3rd) on pH are observed for the 1st (T1) site and the 3rd site assigned to involvement of two acidic amino acids, Asp105 and Glu463. Potential difference between cathodic peaks of BOD as a dependence on pH, overview
additional information
immobilization of bilirubin oxidase on graphene oxide flakes with different negative charge density for oxygen reduction, effect of graphene oxide charge density on enzyme coverage, electron transfer rate and current density. An effective bilirubin oxidase-based biocathode using graphene oxide can be prepared in 2 steps: 1. electrostatic adsorption of the enzyme on graphene oxide, 2. electrochemical reduction of the enzyme-elektrode composite to form a electrochemically reduced graphene oxide-enzyme film (BOD-ErGO) on the electrode, identification of an optimal charge density of graphene oxide for BOD-ErGO composite preparation, method evaluation and electrode characterization, detailed overview. Results reveal that 1. there is an optimal density of a negative surface charge density needed to obtain high j, GAMMA and kS, 2. a lower negative surface charge density is needed to achieve the highest kS compared to j, GAMMA, and 3. current density is influenced mainly by GAMMA and to lesser extent by kS, suggesting that the electron exchange in all cases is fast enough for not being a limiting factor in a biocatalytic current generation
additional information
mediator-free direct electron transfer (DET)-type of immobilization between biocatalysts and electrode surface is achieved by favorable adsorption of BOD on solid surfaces: electrochemical conditioning of aminocarbon nanotubes on a graphene support in an alkaline solution is used to produce -NHOH as hydrophilic functional groups for the efficient immobilization of bilirubin oxidase enzyme. Application of the immobilized enzyme for direct electrocatalytic reduction of O2 is investigated. The onset potential of 0.81 V versus NHE and peak current density of 2.3 mAcm2 for rotating modified electrode at 1250 rpm indicate improved biocatalytic activity of the proposed system for O2 reduction, immobilization of the enzyme on target amino-CNT-Gr modified electrode, method evaluation, detailed overview
additional information
mediator-less, direct electro-catalytic reduction of oxygen to water is achieved on spectrographite electrodes modified by physical adsorption of bilirubin oxidases from Myrothecium verrucaria. The existence of an alternative resting form of the enzyme is validated. Effects on the catalytic cycle by temperature, pH and the presence of halogens in the buffer, overview
additional information
-
mediator-less, direct electro-catalytic reduction of oxygen to water is achieved on spectrographite electrodes modified by physical adsorption of bilirubin oxidases from Myrothecium verrucaria. The existence of an alternative resting form of the enzyme is validated. Effects on the catalytic cycle by temperature, pH and the presence of halogens in the buffer, overview
additional information
immobilization of the enzyme on a mesoporous carbon cryogel electrode, allowing a direct electron transfer (DET) from the carbon electrode to the type I copper site of the enzyme, and analysis of the bioelectrocatalytic reactions of the enzyme in presence and absence of a mediator. The current from the dioxygenreduction reaction (ORR), catalyzed by enzyme BOD, depends on the temperature and pH of the electrolyte.The mediated ORR catalyzed by BOD on CCG electrode is also investigated using osmium-based redox polymers. The catalytic current on the CCG electrode modified with 0.2 mg/cm2 of hydrogel consisting of an enzyme, a redox polymer and a cross linker, is 1.8 mA/cm2, which is almost five times higher than that on a flat glassy carbon electrode for the same hydrogel composition and loading. The catalytic current linearly increases with the total amount of hydrogel on the porous carbon electrode while the catalytic current on the flat electrode is indifferent to the loading. Method evaluation, detailed overview
additional information
-
immobilization of the enzyme on a mesoporous carbon cryogel electrode, allowing a direct electron transfer (DET) from the carbon electrode to the type I copper site of the enzyme, and analysis of the bioelectrocatalytic reactions of the enzyme in presence and absence of a mediator. The current from the dioxygenreduction reaction (ORR), catalyzed by enzyme BOD, depends on the temperature and pH of the electrolyte.The mediated ORR catalyzed by BOD on CCG electrode is also investigated using osmium-based redox polymers. The catalytic current on the CCG electrode modified with 0.2 mg/cm2 of hydrogel consisting of an enzyme, a redox polymer and a cross linker, is 1.8 mA/cm2, which is almost five times higher than that on a flat glassy carbon electrode for the same hydrogel composition and loading. The catalytic current linearly increases with the total amount of hydrogel on the porous carbon electrode while the catalytic current on the flat electrode is indifferent to the loading. Method evaluation, detailed overview
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Murao, S.; Tanaka, N.
Isolation and identification of a microorganism producing bilirubin oxidase
Agric. Biol. Chem.
46
2031-2034
1982
Albifimbria verrucaria, Striaticonidium cinctum, Paramyrothecium roridum
-
brenda
Tanaka, N.; Murao, S.
Purification and some properties of bilirubin oxidase of Myrotheticum verrucaria MT-1
Agric. Biol. Chem.
46
2499-2503
1982
Albifimbria verrucaria
-
brenda
Yokosuka, O.; Billing, B.
Enzymatic oxidation of bilirubin by intestinal mucosa
Biochim. Biophys. Acta
923
268-274
1987
Rattus norvegicus
brenda
Gotoh, Y.; Kondo, Y.; Kaji, H.; Takeda, A.; Samejima, T.
Characterization of copper atoms in bilirubin oxidase by spectroscopic analyses
J. Biochem.
106
621-626
1989
Albifimbria verrucaria
brenda
Sung, C.; Lavin, A.; Klibanov, A.M.; Langer, R.
An immobilized enzyme reactor for the detoxification of bilirubin
Biotechnol. Bioeng.
28
1531-1539
1986
Albifimbria verrucaria
brenda
Cardenas-Vazquez, R.; Yokosuka, O.; Billing, B.H.
Enzymic oxidation of unconjugated bilirubin by rat liver
Biochem. J.
236
625-633
1986
Rattus norvegicus
brenda
Murao, S.; Tanaka, N.
A new enzyme "bilirubin oxidase" produced by Myrotheticum verrucaria MT-1
Agric. Biol. Chem.
45
2383-2384
1981
Albifimbria verrucaria
-
brenda
Tanaka, N.; Murao, S.
Difference between various copper-containing enzymes (Polyporus laccase, mushroom tyrosinase and cucumber ascorbate oxidase) and bilirubin oxidase
Agric. Biol. Chem.
47
1627-1628
1983
Albifimbria verrucaria, Albifimbria verrucaria MT-1
-
brenda
Skrika-Alexopoulos, E.; Freedman, R.B.
Factors affecting enzyme characteristics of bilirubin oxidase suspensions in organic solvents
Biotechnol. Bioeng.
41
887-893
1993
Albifimbria verrucaria
brenda
Skrika-Alexopoulos, E.; Muir, J.; Freedman, R.B.
Stability of bilirubin oxidase in organic solvent media: A comparative study on two low-water systems
Biotechnol. Bioeng.
41
894-899
1993
Albifimbria verrucaria
brenda
Koikeda, S.; Ando, K.; Kaji, H.; Inoue, T.; Murao, S.; Takeuchi, K.; Samejima, T.
Molecular cloning of the gene for bilirubin oxidase from Myrothecium verrucaria and its expression in yeast
J. Biol. Chem.
268
18801-18809
1993
Albifimbria verrucaria
brenda
Male, K.B.; Luong, J.H.T.
Characterization and kinetic studies of a novel dye prepared from the oxidation of a water-soluble 1,1'-dimethylferrocene-2-hydroxypropyl-.beta-cyclodextrin complex using immobilized bilirubin oxidase
Enzyme Microb. Technol.
16
425-431
1994
Albifimbria verrucaria
-
brenda
Samejima, T.; Wu, C.S.; Shiboya, K.; Kaji, H.; Koikeda, S.; Ando, K.; Yang, J.T.
Conformation of bilirubin oxidase in native and denatured states
J. Protein Chem.
13
307-313
1994
Albifimbria verrucaria
brenda
Xu, F.; Shin, W.; Brown, S.H.; Wahleithner, J.A.; Sundaram, U.M.; Solomon, E.I.
A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
Biochim. Biophys. Acta
1292
303-311
1996
Albifimbria verrucaria
brenda
Nakai, Y.; Yoshioka, S.; Aso, Y.; Kojima, S.
Solid-state rehydration-induced recovery of bilirubin oxidase activity in lyophilized formulations reduced during freeze-drying
Chem. Pharm. Bull.
46
1031-1033
1998
Albifimbria verrucaria
-
brenda
Chen, J.P.; Wang, H.Y.
Improved properties of bilirubin oxidase by entrapment in alginate-silicate sol-gel matrix
Biotechnol. Tech.
12
851-853
1998
Albifimbria verrucaria
brenda
Zhou, X.M.; Liu, J.W.; Zou, X.; Chen, J.J.
Monitoring catalytic reaction of bilirubin oxidase and determination of bilirubin and bilirubin oxidase activity by capillary electrophoresis
Electrophoresis
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Albifimbria verrucaria
brenda
Shimizu, A.; Kwon, J.H.; Sasaki, T.; Satoh, T.; Sakurai, N.; Sakurai, T.; Yamaguchi, S.; Samejima, T.
Myrothecium verrucaria Bilirubin Oxidase and Its Mutants for Potential Copper Ligands
Biochemistry
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Albifimbria verrucaria
brenda
Yoshioka, S.; Aso, Y.; Kojima, S.; Tanimoto, T.
Effect of polymer excipients on the enzyme activity of lyophilized bilirubin oxidase and beta-galactosidase formulations
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Albifimbria verrucaria
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Itoh, S.; Kusaka, T.; Imai, T.; Isobe, K.; Onishi, S.
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Albifimbria verrucaria
brenda
Kim, H.H.; Zhang, Y.; Heller, A.
Bilirubin oxidase label for an enzyme-linked affinity assay with O2 as substrate in a neutral pH NACL solution
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Albifimbria verrucaria
brenda
Kang, C.; Shin, H.; Zhang, Y.; Heller, A.
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Bioelectrochemistry
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brenda
Sakurai, T.; Zhan, L.; Fujita, T.; Kataoka, K.; Shimizu, A.; Samejima, T.; Yamaguchi, S.
Authentic and recombinant bilirubin oxidases are in different resting forms
Biosci. Biotechnol. Biochem.
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Albifimbria verrucaria
brenda
Zoppellaro, G.; Sakurai, N.; Kataoka, K.; Sakurai, T.
The reversible change in the redox state of type I Cu in Myrothecium verrucaria bilirubin oxidase depending on pH
Biosci. Biotechnol. Biochem.
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2004
Albifimbria verrucaria
brenda
Shimizu, A.; Samejima, T.; Hirota, S.; Yamaguchi, S.; Sakurai, N.; Sakurai, T.
Type III Cu mutants of Myrothecium verrucaria bilirubin oxidase
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Albifimbria verrucaria
brenda
Tsujimura, S.; Kano, K.; Ikeda, T.
Bilirubin oxidase in multiple layers catalyzes four-electron reduction of dioxygen to water without redox mediators
J. Electroanal. Chem.
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Myrothecium sp.
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Kataoka, K.; Tanaka, K.; Sakai, Y.; Sakurai, T.
High-level expression of Myrothecium verrucaria bilirubin oxidase in Pichia pastoris, and its facile purification and characterization
Protein Expr. Purif.
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Albifimbria verrucaria
brenda
Sakasegawa, S.; Ishikawa, H.; Imamura, S.; Sakuraba, H.; Goda, S.; Ohshima, T.
Bilirubin oxidase activity of Bacillus subtilis CotA
Appl. Environ. Microbiol.
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Bacillus subtilis
brenda
Kataoka, K.; Kitagawa, R.; Inoue, M.; Naruse, D.; Sakurai, T.; Huang, H.W.
Point mutations at the type I Cu ligands, Cys457 and Met467, and at the putative proton donor, Asp105, in Myrothecium verrucaria bilirubin oxidase and reactions with dioxygen
Biochemistry
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2005
Albifimbria verrucaria
brenda
Christenson, A.; Shleev, S.; Mano, N.; Heller, A.; Gorton, L.
Redox potentials of the blue copper sites of bilirubin oxidases
Biochim. Biophys. Acta
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2006
Ganoderma tsunodae, Albifimbria verrucaria (Q12737), Albifimbria verrucaria
brenda
Zhang, L.; Zhang, X.; Luo, Z.Y.
Value of bilirubin oxidase and its mutants in the diagnosis of hyperbilirubinemia
Di Yi Jun Yi Da Xue Xue Bao
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2005
Aspergillus oryzae
brenda
Otsuka, K.; Sugihara, T.; Tsujino, Y.; Osakai, T.; Tamiya, E.
Electrochemical consideration on the optimum pH of bilirubin oxidase
Anal. Biochem.
370
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2007
Albifimbria verrucaria, Albifimbria verrucaria BO3
brenda
Ikeda, T.; Tatsumi, H.; Katano, H.; Wanibuchi, M.; Hibi, T.; Kajino, T.
A bioelectrocatalysis method for the kinetic measurement of thermal inactivation of a redox enzyme, bilirubin oxidase
Anal. Sci.
24
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2008
Albifimbria verrucaria
brenda
Dronov, R.; Kurth, D.G.; Moehwald, H.; Scheller, F.W.; Lisdat, F.
Communication in a protein stack: electron transfer between cytochrome c and bilirubin oxidase within a polyelectrolyte multilayer
Angew. Chem.
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2008
Albifimbria verrucaria
brenda
Kataoka, K.; Tsukamoto, K.; Kitagawa, R.; Ito, T.; Sakurai, T.
Compensatory binding of an asparagine residue to the coordination-unsaturated type I Cu center in bilirubin oxidase mutants
Biochem. Biophys. Res. Commun.
371
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2008
Albifimbria verrucaria
brenda
Ramirez, P.; Mano, N.; Andreu, R.; Ruzgas, T.; Heller, A.; Gorton, L.; Shleev, S.
Direct electron transfer from graphite and functionalized gold electrodes to T1 and T2/T3 copper centers of bilirubin oxidase
Biochim. Biophys. Acta
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2008
Ganoderma tsunodae
brenda
Ivnitski, D.; Artyushkova, K.; Atanassov, P.
Surface characterization and direct electrochemistry of redox copper centers of bilirubin oxidase from fungi Myrothecium verrucaria
Bioelectrochemistry
74
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2008
Albifimbria verrucaria
brenda
Sakurai, T.; Kataoka, K.
Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase
Chem. Rec.
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2007
Albifimbria verrucaria
brenda
Dronov, R.; Kurth, D.G.; Scheller, F.W.; Lisdat, F.
Direct and cytochrome c mediated electrochemistry of bilirubin oxidase on gold
Electroanalysis
19
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2007
Albifimbria verrucaria
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brenda
Shin, H.; Kang, C.; Heller, A.
Irreversible and reversible deactivation of bilirubin oxidase by urate
Electroanalysis
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2007
Ganoderma tsunodae
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brenda
Weigel, M.C.; Tritscher, E.; Lisdat, F.
Direct electrochemical conversion of bilirubin oxidase at carbon nanotube-modified glassy carbon electrodes
Electrochem. Commun.
9
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2007
Albifimbria verrucaria
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brenda
Liu, Y.; Zhang, X.; Yan, K.; Wang, H.; Wu, H.
Decolorization of indigo carmine by crude bilirubin oxidase from Myrothecium sp
Fresenius Environ. Bull.
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Myrothecium sp.
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brenda
Zhang, X.; Liu, Y.; Yan, K.; Wu, H.
Decolorization of anthraquinone-type dye by bilirubin oxidase-producing nonligninolytic fungus Myrothecium sp. IMER1
J. Biosci. Bioeng.
104
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2007
Myrothecium sp., Myrothecium sp. IMER1
brenda
Kamitaka, Y.; Tsujimura, S.; Kataoka, K.; Sakurai, T.; Ikeda, T.; Kano, K.
Effects of axial ligand mutation of the type I copper site in bilirubin oxidase on direct electron transfer-type bioelectrocatalytic reduction of dioxygen
J. Electroanal. Chem.
601
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2007
Albifimbria verrucaria
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brenda
Lim, J.; Cirigliano, N.; Wang, J.; Dunn, B.
Direct electron transfer in nanostructured sol-gel electrodes containing bilirubin oxidase
Phys. Chem. Chem. Phys.
9
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2007
Albifimbria verrucaria
brenda
Katano, H.; Tatsumi, H.; Hibi, T.; Ikeda, T.; Tsukatani, T.
Application of polyammonium cations to enzyme-immobilized electrode: application as enzyme stabilizer for bilirubin oxidase
Anal. Sci.
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2008
Albifimbria verrucaria
brenda
Katano, H.; Uematsu, K.; Hibi, T.; Ikeda, T.; Tsukatani, T.
Application of poly[oxyethylene(dimethylimino)propyl-(dimethylimino)ethylene] as enzyme stabilizer for bilirubin oxidase immobilized electrode
Anal. Sci.
25
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2009
Albifimbria verrucaria
brenda
Mizutani, K.; Toyoda, M.; Sagara, K.; Takahashi, N.; Sato, A.; Kamitaka, Y.; Tsujimura, S.; Nakanishi, Y.; Sugiura, T.; Yamaguchi, S.; Kano, K.; Mikami, B.
X-ray analysis of bilirubin oxidase from Myrothecium verrucaria at 2.3 A resolution using a twinned crystal
Acta Crystallogr. Sect. F
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2010
Albifimbria verrucaria (Q12737), Albifimbria verrucaria, Albifimbria verrucaria MT-1 (Q12737)
brenda
Ikeda, T.; Uematsu, K.; Ma, H.; Katano, H.; Hibi, T.
Measurements of reversible and irreversible inactivation processes of a redox enzyme, bilirubin oxidase, by electrochemical methods based on bioelectrocatalysis
Anal. Sci.
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2009
Albifimbria verrucaria
brenda
Iwaki, M.; Kataoka, K.; Kajino, T.; Sugiyama, R.; Morishita, H.; Sakurai, T.
ATR-FTIR study of the protonation states of the Glu residue in the multicopper oxidases, CueO and bilirubin oxidase
FEBS Lett.
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2010
Albifimbria verrucaria (Q12737)
brenda
Liu, Y.; Huang, J.; Zhang, X.
Decolorization and biodegradation of remazol brilliant blue R by bilirubin oxidase
J. Biosci. Bioeng.
108
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2009
Albifimbria verrucaria, Albifimbria verrucaria IMER1
brenda
Dos Santos, L.; Climent, V.; Blanford, C.F.; Armstrong, F.A.
Mechanistic studies of the blue Cu enzyme, bilirubin oxidase, as a highly efficient electrocatalyst for the oxygen reduction reaction
Phys. Chem. Chem. Phys.
12
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2010
Albifimbria verrucaria
brenda
Durand, F.; Gounel, S.; Kjaergaard, C.H.; Solomon, E.I.; Mano, N.
Bilirubin oxidase from Magnaporthe oryzae: an attractive new enzyme for biotechnological applications
Appl. Microbiol. Biotechnol.
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2012
Pyricularia oryzae, Pyricularia oryzae ATCC MYA-4617
brenda
Mano, N.
Features and applications of bilirubin oxidases
Appl. Microbiol. Biotechnol.
96
301-307
2012
Aspergillus sojae, Penicillium janthinellum, Pyricularia oryzae, Ganoderma tsunodae, Bacillus pumilus (A8FAG9), Bacillus subtilis (P07788), Albifimbria verrucaria (Q12737), Bacillus licheniformis (Q65MU7), Pleurotus ostreatus (Q9UVY4)
brenda
Durand, F.; Kjaergaard, C.H.; Suraniti, E.; Gounel, S.; Hadt, R.G.; Solomon, E.I.; Mano, N.
Bilirubin oxidase from Bacillus pumilus: a promising enzyme for the elaboration of efficient cathodes in biofuel cells
Biosens. Bioelectron.
35
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2012
Bacillus pumilus
brenda
Han, X.; Zhao, M.; Lu, L.; Liu, Y.
Purification, characterization and decolorization of bilirubin oxidase from Myrothecium verrucaria 3.2190
Fungal Biol.
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Albifimbria verrucaria, Albifimbria verrucaria 3.2190
brenda
Khlupova, M.E.; Vasileva, I.S.; Shumakovich, G.P.; Morozova, O.V.; Chertkov, V.A.; Shestakova, A.K.; Kisin, A.V.; Yaropolov, A.I.
Enzymatic polymerization of dihydroquercetin using bilirubin oxidase
Biochemistry (Moscow)
80
233-241
2015
Albifimbria verrucaria (Q12737)
brenda
Santoro, C.; Babanova, S.; Erable, B.; Schuler, A.; Atanassov, P.
Bilirubin oxidase based enzymatic air-breathing cathode operation under pristine and contaminated conditions
Bioelectrochemistry
108
1-7
2016
Albifimbria verrucaria (Q12737)
brenda
Filip, J.; Tkac, J.
The pH dependence of the cathodic peak potential of the active sites in bilirubin oxidase
Bioelectrochemistry
96
14-20
2014
Albifimbria verrucaria (Q12737)
brenda
Filip, J.; Andicsova-Eckstein, A.; Vikartovska, A.; Tkac, J.
Immobilization of bilirubin oxidase on graphene oxide flakes with different negative charge density for oxygen reduction. The effect of GO charge density on enzyme coverage, electron transfer rate and current density
Biosens. Bioelectron.
89
384-389
2017
Albifimbria verrucaria (Q12737)
brenda
Navaee, A.; Salimi, A.; Jafari, F.
Electrochemical pretreatment of amino-carbon nanotubes on graphene support as a novel platform for bilirubin oxidase with improved bioelectrocatalytic activity towards oxygen reduction
Chemistry
21
4949-4953
2015
Albifimbria verrucaria (Q12737)
brenda
Tsujimura, S.; Murata, K.
Electrochemical oxygen reduction catalyzed by bilirubin oxidase with the aid of 2,2'-azinobis(3-ethylbenzothiazolin-6-sulfonate) on a MgO-template carbon electrode
Electrochim. Acta
180
555-559
2015
Bacillus pumilus (A8FAG9), Bacillus pumilus SAFR-032 (A8FAG9)
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brenda
Gounel, S.; Rouhana, J.; Stines-Chaumeil, C.; Cadet, M.; Mano, N.
Increasing the catalytic activity of bilirubin oxidase from Bacillus pumilus importance of host strain and chaperones proteins
J. Biotechnol.
230
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2016
Bacillus pumilus (A8FAG9), Bacillus pumilus, Bacillus pumilus SAFR-032 (A8FAG9)
brenda
Tasca, F.; Farias, D.; Castro, C.; Acuna-Rougier, C.; Antiochia, R.
Bilirubin oxidase from Myrothecium verrucaria physically absorbed on graphite electrodes. Insights into the alternative resting form and the sources of activity loss
PLoS ONE
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e0132181
2015
Albifimbria verrucaria (Q12737), Albifimbria verrucaria
brenda
Yamamoto, K.; Matsumoto, T.; Shimada, S.; Tanaka, T.; Kondo, A.
Starchy biomass-powered enzymatic biofuel cell based on amylases and glucose oxidase multi-immobilized bioanode
New Biotechnol.
30
531-535
2013
Albifimbria verrucaria (Q12737)
brenda
Kataoka, K.; Ito, T.; Okuda, Y.; Sakai, Y.; Yamashita, S.; Sakurai, T.
Roles of the indole ring of Trp396 covalently bound with the imidazole ring of His398 coordinated to type I copper in bilirubin oxidase
Biochem. Biophys. Res. Commun.
521
620-624
2020
Albifimbria verrucaria
brenda
Tsujimura, S.
From fundamentals to applications of bioelectrocatalysis bioelectrocatalytic reactions of FAD-dependent glucose dehydrogenase and bilirubin oxidase
Biosci. Biotechnol. Biochem.
83
39-48
2019
Albifimbria verrucaria
brenda
Tang, J.; Yan, X.; Huang, W.; Engelbrekt, C.; Duus, J.O.; Ulstrup, J.; Xiao, X.; Zhang, J.
Bilirubin oxidase oriented on novel type three-dimensional biocathodes with reduced graphene aggregation for biocathode
Biosens. Bioelectron.
167
112500
2020
Albifimbria verrucaria
brenda
Takimoto, D.; Tsujimura, S.
Oxygen reduction reaction activity and stability of electrochemically deposited bilirubin oxidase
Chem. Lett.
47
1269-1271
2018
Albifimbria verrucaria
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brenda
Akter, M.; Tokiwa, T.; Shoji, M.; Nishikawa, K.; Shigeta, Y.; Sakurai, T.; Higuchi, Y.; Kataoka, K.; Shibata, N.
Redox potential-dependent formation of an unusual His-Trp bond in bilirubin oxidase
Chemistry
24
18052-18058
2018
Albifimbria verrucaria
brenda
Roucher, A.; Roussarie, E.; Gauvin, R.M.; Rouhana, J.; Gounel, S.; Stines-Chaumeil, C.; Mano, N.; Backov, R.
Bilirubin oxidase-based silica macrocellular robust catalyst for on line dyes degradation
Enzyme Microb. Technol.
120
77-83
2019
Bacillus pumilus (A8FAG9), Bacillus pumilus, Bacillus pumilus SAFR-032 (A8FAG9)
brenda
Rawal, R.; Kharangarh, P.R.; Dawra, S.; Bhardwaj, P.
Synthesis, characterization and immobilization of bilirubin oxidase nanoparticles (BOxNPs) with enhanced activity Application for serum bilirubin determination in jaundice patients
Enzyme Microb. Technol.
143
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2021
Albifimbria verrucaria
brenda
Gross, A.J.; Chen, X.; Giroud, F.; Travelet, C.; Borsali, R.; Cosnier, S.
Redox-active glyconanoparticles as electron shuttles for mediated electron transfer with bilirubin oxidase in solution
J. Am. Chem. Soc.
139
16076-16079
2017
Albifimbria verrucaria
brenda
Bayineni, V.K.; Suresh, S.; Sharma, A.; Kadeppagari, R.K.
Improvement of bilirubin oxidase productivity of Myrothecium verrucaria and studies on the enzyme overproduced by the mutant strain in the solid-state fermentation
J. Gen. Appl. Microbiol.
64
68-75
2018
Albifimbria verrucaria, Albifimbria verrucaria MTCC 2140
brenda
Tokiwa, T.; Shoji, M.; Sladek, V.; Shibata, N.; Higuchi, Y.; Kataoka, K.; Sakurai, T.; Shigeta, Y.; Misaizu, F.
Structural changes of the trinuclear copper center in bilirubin oxidase upon reduction
Molecules
24
76
2018
Albifimbria verrucaria
brenda
Sadeghian, I.; Rezaie, Z.; Rahmatabadi, S.; Hemmati, S.
Biochemical insights into a novel thermo/organo tolerant bilirubin oxidase from Thermosediminibacter oceani and its application in dye decolorization
Process Biochem.
88
38-50
2020
Thermosediminibacter oceani (D9RY72), Thermosediminibacter oceani DSM 16646 (D9RY72)
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brenda
Hasan, M.Q.; Kuis, R.; Narayanan, J.S.; Slaughter, G.
Fabrication of highly effective hybrid biofuel cell based on integral colloidal platinum and bilirubin oxidase on gold support
Sci. Rep.
8
16351
2018
Albifimbria verrucaria
brenda
Koval, T.; Svecova, L.; Ostergaard, L.H.; Skalova, T.; Duskova, J.; Hasek, J.; Kolenko, P.; Fejfarova, K.; Stransky, J.; Trundova, M.; Dohnalek, J.
Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer
Sci. Rep.
9
13700
2019
Albifimbria verrucaria (Q12737), Albifimbria verrucaria, Albifimbria verrucaria ATCC24571 (Q12737)
brenda