1.3.3.5: bilirubin oxidase
This is an abbreviated version!
For detailed information about bilirubin oxidase, go to the full flat file.
Word Map on EC 1.3.3.5
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1.3.3.5
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electrode
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oxidases
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biofuel
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cathode
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ceruloplasmin
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myrothecium
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anode
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laccases
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verrucaria
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biocathode
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ferroxidase
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trinuclear
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abts
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laccase-like
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dioxygen
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bioanode
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electrocatalytic
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bioelectrocatalytic
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2,6-dimethoxyphenol
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biliverdin
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cuprous
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multi-copper
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syringaldazine
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copa
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copper-binding
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four-electron
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mniii
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self-powered
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aceruloplasminemia
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hephaestin
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p-phenylenediamine
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manganeseii
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bioelectrodes
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open-circuit
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membrane-less
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cupredoxins
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analysis
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electrocatalysts
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manganese-oxidizing
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methionine-rich
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diazo
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biodevice
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energy production
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medicine
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diagnostics
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biotechnology
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synthesis
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environmental protection
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industry
- 1.3.3.5
-
electrode
- oxidases
-
biofuel
-
cathode
- ceruloplasmin
- myrothecium
-
anode
- laccases
- verrucaria
-
biocathode
- ferroxidase
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trinuclear
- abts
-
laccase-like
- dioxygen
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bioanode
-
electrocatalytic
-
bioelectrocatalytic
- 2,6-dimethoxyphenol
- biliverdin
-
cuprous
-
multi-copper
- syringaldazine
- copa
-
copper-binding
-
four-electron
-
mniii
-
self-powered
-
aceruloplasminemia
- hephaestin
- p-phenylenediamine
-
manganeseii
-
bioelectrodes
-
open-circuit
-
membrane-less
- cupredoxins
- analysis
-
electrocatalysts
-
manganese-oxidizing
-
methionine-rich
-
diazo
-
biodevice
- energy production
- medicine
- diagnostics
- biotechnology
- synthesis
- environmental protection
- industry
Reaction
2 bilirubin
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Synonyms
bilirubin oxidase, bilirubin oxidase M-1, bilirubin:oxygen oxidoreductase, blue Cu enzyme, BOD, BODx, BOX, BPUM_0542, copper oxidase, CotA, MCO, multicopper oxidase, MvBO, MvBOD, oxidase, bilirubin
ECTree
1.3.3.5 bilirubin oxidaseAdvanced search results
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results (Engineering
Engineering on EC 1.3.3.5 - bilirubin oxidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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
C457S
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can react with dioxygen, affords reaction intermediate I with absorption maxima at 340, 470, and 675 nm
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
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
M467F
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the mutated type I Cu center shows characteristics of phytocyanins
M467G
M467L
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the mutated type I Cu center shows characteristics of phytocyanins
M467Q
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
W396A
W396D
the mutant shows practically zero activity compared to the wild type enzyme
W396F
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
Albifimbria verrucaria ATCC24571
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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
Albifimbria verrucaria ATCC24571
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the mutant shows practically zero activity compared to the wild type enzyme
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W396F
Albifimbria verrucaria ATCC24571
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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
additional information
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
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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
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
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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
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
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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
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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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