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Information on EC 1.1.99.11 - fructose 5-dehydrogenase
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1.1.99.11 fructose 5-dehydrogenaseIUBMB Comments
2,6-Dichloroindophenol can act as acceptor.
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Word Map
- 1.1.99.11
-
electrode
-
biosensors
-
amperometric
- gluconobacter
-
tetrathiafulvalene
- 5-keto-d-fructose
-
bioanode
-
biocathode
-
bioelectrode
-
screen-printed
-
bioelectrocatalysts
-
one-compartment
-
det-type
-
open-circuit
-
transfer-type
-
alkanethiolate
- biotechnology
- industry
- analysis
The expected taxonomic range for this enzyme is: Gluconobacter
Synonyms
D-fructose dehydrogenase, dehydrogenase, fructose 5- (acceptor), FDH, FdhL, FdhS, fdhSCL, fructose 5-dehydrogenase, fructose dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D-fructose dehydrogenase
dehydrogenase, fructose 5- (acceptor)
-
-
-
-
FDH
FdhL
FdhS
fdhSCL
fructose dehydrogenase
D-fructose dehydrogenase
-
-
-
-
FDH
-
-
-
-
FDH
-
-
fdhSCL
-
gene name of the flavoprotein-cytochrome c complex fructose dehydrogenase
fdhSCL
-
gene name of the flavoprotein-cytochrome c complex fructose dehydrogenase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
-
-
-
-
D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor
ping-pong mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
D-fructose:acceptor 5-oxidoreductase
2,6-Dichloroindophenol can act as acceptor.
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CAS REGISTRY NUMBER
COMMENTARY
37250-85-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-fructose + 1,1'-dimethylferricenium ion
5-dehydro-D-fructose + 1,1'-dimethylferrocenium ion
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
D-fructose + 7,7,8,8-tetracyanoquinodimethane
5-dehydro-D-fructose + reduced 7,7,8,8-tetracyanoquinodimethane
-
-
-
-
?
D-fructose + acceptor
2-dehydro-D-fructose + reduced acceptor
-
direct electron-transfer bioelectrocatalytic oxidation, DET-type
-
-
?
D-fructose + oxidized 1-methoxy-5-methylphenazinium methylsulfate
5-dehydro-D-fructose + reduced 1-methoxy-5-methylphenazinium methylsulfate
-
-
-
-
?
D-fructose + [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide]
5-dehydro-D-fructose + [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan
-
in the presence of phenazine methosulfate
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-farnesyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinone
5-dehydro-D-fructose + 2,3-dimethoxy-5-methyl-1,4-benzoquinol
-
-
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
most effective electron acceptor
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-fructose + 2,6-dichlorophenolindophenol
5-dehydro-D-fructose + reduced 2,6-dichlorophenolindophenol
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
involved in utilization of D-fructose by acetic acid bacteria
-
-
-
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + ferricyanide
5-dehydro-D-fructose + ferrocyanide
-
-
-
-
?
D-fructose + nitro blue tetrazolium
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + nitro blue tetrazolium
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + phenazine methosulfate
5-dehydro-D-fructose + ?
-
-
-
?
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
additional information
?
-
-
oxygen is completely inactive as an electron acceptor
-
-
-
additional information
?
-
-
when FDH is adsorbed onto a porous carbon electrode surface, it can transfer electrons from D-fructose to the electrode directly without a mediator
-
-
-
additional information
?
-
-
cells producing only subunits FdhS and FdhL have no fructose-oxidizing activity, but show significantly high D-fructose:ferricyanide oxidoreductase activity in the soluble fraction of cell extracts, whereas the cells producing the FDH complex show activity in the membrane fraction
-
-
-
additional information
?
-
-
cells producing only subunits FdhS and FdhL have no fructose-oxidizing activity, but show significantly high D-fructose:ferricyanide oxidoreductase activity in the soluble fraction of cell extracts, whereas the cells producing the FDH complex show activity in the membrane fraction
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
oxygen is completely inactive as an electron acceptor
-
-
-
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
involved in utilization of D-fructose by acetic acid bacteria
-
-
-
D-fructose + acceptor
5-dehydro-D-fructose + reduced acceptor
-
-
-
-
?
D-fructose + ubiquinone
5-dehydro-D-fructose + ubiquinol
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyrroloquinoline quinone
-
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
cytochrome c
-
contains a cytochrome c like electron carrier, tightly bound
cytochrome c
-
the cytochrome c subunit is responsible not only for membrane anchoring but also for ubiquinone reduction
heme
-
quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10
D-fructose
-
in presence of 2,6-dichlorophenolindophenol, 67 mM, pH 5.5, 15°C
10
D-fructose
-
irreversibly adsorbed on Ketjen black - modified glassy carbon electrodes
11
D-fructose
-
Km is determined using FDH adsorbed onto multi-walled carbon nanotubes synthesized on platinum electrode
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6.4
-
pH 4.5: about 85% of maximal activity, pH 6.4: about 50% of maximal activity
4.5 - 6.5
-
enzymatic activity is significantly inhibited at pH lower than 4.5 or higher than 6.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (278 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
16000
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
19700
49000
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
50800
51000
60000
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence
67000
140000
19700
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
50800
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
67000
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
trimer
-
1 * 67000, flavin dehydrogenase, + 1 * 50800, cytochrome c, + 1 * 19700, subunit of unknown function, SDS-PAGE
heterotrimer
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence; 1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
heterotrimer
-
1 * 60000 + 1 * 49000 + 1 * 16000, calculated from amino acid sequence; 1 * 67000 + 1 * 51000 + 1 * 20000, SDS-PAGE; 1 * 68000 + 1 * 51000 + 1 * 18000, SDS-PAGE
-
heterotrimer
-
1 * 67000 + 1 * 50800 + 1 * 19700, calculated from amino acid sequence
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25°C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme immobilized onto giant vesicles is stable for at least 20 days at 25°C, while the activity of the free enzyme dropps to about 20% of its initial activity during the same period of time
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0-4°C, pH 4.0-5.0, 0.1% Triton X-100, 1 mM 2-mercaptoethanol, for at least 2 weeks
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, DEAE-Sepharose column chromatography, Toyopearl CM-650 column chromatography, and Superdex 200 gel filtration
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
the enzyme is a satisfactory reagent for microdetermination of D-fructose
biotechnology
industry
-
direct electron-transfer bioelectrocatalysis can be used in biosensors, biofuel cells and bioreactors, FDH immobilised on Ketjen black electroconductive material produces a catalytic oxidation wave of D-fructose without a mediator, the electron in FDH seems to be directly transferred to the electrode via the heme c site
biotechnology
-
multi-walled carbon nanotubes synthesized on platinum plate (MWCNTs/Pt) electrode are immediately immersed into solutions of FDH to immobilize the enzyme onto electrode surfaces. Thereafter, a well-defined catalytic oxidation current based on FDH is observed from ca. -0.15V, which is close to the redox potential of heme c as a prosthetic group of FDH. From an analysis of a plot of the catalytic current versus substrate, the calibration range for the fructose concentration is up to ca. 40 mmol/dm3, and the apparent Michaelis-Menten constant is evaluated to be 11 mmol/l. The obtained results are useful in applications to prepare the third-generation biosensors and other future bioelectrochemical devices
biotechnology
-
an automated, enzymatic insulin assay is developed. Principle: Fructose is produced by the action of inulinase on inulin present in the sample. The resulting fructose reacts with D-fructose dehydrogenase in the presence of the oxidized form of 1-methoxy-5-methylphenazinium methylsulfate (1-m-PMS) to produce the reduced form of 1-m-PMS. Reduced 1-m-PMS acts on dissolved oxygen to produce hydrogen peroxide, which, through the action of peroxidase, oxidatively condenses N-ethyl-N-(2-hydroxy-3-sulfopropyl)-m-toluidine and 4-aminoantipyrine to transform them into quinoneimine dye. The absorbance of the quinoneimine dye is measured spectrophotometrically to determine the concentration of inulin in the sample. The new enzymatic assay offers a more convenient and more accurate measurement of inulin and may be suitable for routine procedures by automated analyzers in clinical laboratories
biotechnology
-
using fructose dehydrogenase-catalyzed conversion of d-fructose to 5-ketofructose, followed by quantitation of MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] formazan production by direct spectrophotometry, an assay to measure serum fructose concentration is developed. The fructose dehydrogenase-based enzymatic assay correlates highly with gas chromatography-mass spectroscopic analysis of serum fructose. The assay is highly specific, exhibits no cross-reactivity with other sugars and is easy to perform
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ameyama, M.; Adachi, O.
D-Fructose dehydrogenase from Gluconobacter industrius, membrane-bound
Methods Enzymol.
89
154-159
1982
Gluconobacter oxydans
-
brenda
Yamada, Y.; Aida, K.; Uemura, T.
Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase
J. Biochem.
61
636-646
1967
Gluconobacter cerinus
brenda
Ameyama, M.; Shinagawa, E.; Matsushita, K.; Adachi, O.
D-Fructose dehydrogenase of Gluconobacter industrius: purification, characterization, and application to enzymatic microdetermination of D-fructose
J. Bacteriol.
145
814-823
1981
Gluconobacter oxydans
brenda
Marcinkeviciene, J.; Johansson, G.
Kinetic studies of the active sites functioning in the quinohemoprotein fructose dehydrogenase
FEBS Lett.
318
23-26
1993
Gluconobacter sp.
brenda
Kato, K.; Walde, P.; Mitsui, H.; Higashi, N.
Enzymatic activity and stability of D-fructose dehydrogenase and sarcosine dehydrogenase immobilized onto giant vesicles
Biotechnol. Bioeng.
84
415-423
2003
Gluconobacter sp.
brenda
Kamitaka, Y.; Tsujimura, S.; Kano, K.
High current density bioelectrolysis of D-fructose at fructose dehydrogenase-adsorbed and Ketjen black-modified electrodes without a mediator
Chem. Lett.
36
218-219
2007
Gluconobacter sp.
-
brenda
Tominaga, M.; Nomura, S.; Taniguchi, I.
D-fructose detection based on the direct heterogeneous electron transfer reaction of fructose dehydrogenase adsorbed onto multi-walled carbon nanotubes synthesized on platinum electrode
Biosens. Bioelectron.
24
1184-1188
2009
Gluconobacter sp.
brenda
Kimata, S.; Mizuguchi, K.; Hattori, S.; Teshima, S.; Orita, Y.
Evaluation of a new automated, enzymatic inulin assay using D-fructose dehydrogenase
Clin. Exp. Nephrol.
13
341-349
2009
Gluconobacter oxydans
brenda
Hui, H.; Huang, D.; McArthur, D.; Nissen, N.; Boros, L.G.; Heaney, A.P.
Direct spectrophotometric determination of serum fructose in pancreatic cancer patients
Pancreas
38
706-712
2009
Gluconobacter sp.
brenda
Tsujimura, S.; Nishina, A.; Kamitaka, Y.; Kano, K.
Coulometric D-fructose biosensor based on direct electron transfer using D-fructose dehydrogenase
Anal. Chem.
81
9383-9387
2009
Gluconobacter frateurii
brenda
Sasaki, Y.; Sugihara, T.; Osakai, T.
Electron transfer mediated by membrane-bound D-fructose dehydrogenase adsorbed at an oil/water interface
Anal. Biochem.
417
129-135
2011
Gluconobacter sp.
brenda
Kawai, S.; Goda-Tsutsumi, M.; Yakushi, T.; Kano, K.; Matsushita, K.
Heterologous overexpression and characterization of a flavoprotein-cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus NBRC3260
Appl. Environ. Microbiol.
79
1654-1660
2013
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
brenda
Sasakura, K.; Shirai, O.; Hichiri, K.; Goda-Tsutsumi, M.; Tsujimura, S.; Kano, K.
Ion transport across planar bilayer lipid membrane driven by D-fructose dehydrogenase-catalyzed electron transport
Chem. Lett.
40
486-488
2011
Gluconobacter sp.
-
brenda
Hickey, D.; Giroud, F.; Schmidtke, D.; Glatzhofer, D.; Minteer, S.
Enzyme cascade for catalyzing sucrose oxidation in a biofuel cell
ACS Catal.
3
2729-2737
2013
Gluconobacter sp.
-
brenda
Sarauli, D.; Wettstein, C.; Peters, K.; Schulz, B.; Fattakhova-Rohlfing, D.; Lisdat, F.
Interaction of fructose dehydrogenase with a sulfonated polyaniline: application for enhanced bioelectrocatalysis
ACS Catal.
5
2081-2087
2015
Gluconobacter japonicus
-
brenda
Wettstein, C.; Kano, K.; Schäfer, D.; Wollenberger, U.; Lisdat, F.
Interaction of flavin-dependent fructose dehydrogenase with cytochrome c as basis for the construction of biomacromolecular architectures on electrodes
Anal. Chem.
88
6382-6389
2016
Gluconobacter japonicus, Gluconobacter japonicus NBRCA3260
brenda
Kawai, S.; Yakushi, T.; Matsushita, K.; Kitazumi, Y.; Shirai, O.; Kano, K.
The electron transfer pathway in direct electrochemical communication of fructose dehydrogenase with electrodes
Electrochem. Commun.
38
28-31
2014
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Funabashi, H.; Murata, K.; Tsujimura, S.
Effect of pore size of MgO-templated carbon on the direct electrochemistry of D-fructose dehydrogenase
Electrochemistry
83
372-375
2015
Gluconobacter japonicus
-
brenda
Hichiri, K.; Shirai, O.; Kitazumi, Y.; Kano, K.
Coupling of proton transport across planar lipid bilayer and electron transport catalyzed by membrane-bound enzyme D-fructose dehydrogenase
Electrochemistry
84
328-333
2016
Gluconobacter japonicus
-
brenda
Kawai, S.; Yakushi, T.; Matsushita, K.; Kitazumi, Y.; Shirai, O.; Kano, K.
Role of a non-ionic surfactant in direct electron transfer-type bioelectrocatalysis by fructose dehydrogenase
Electrochim. Acta
152
19-24
2015
Gluconobacter japonicus
-
brenda
Sugimoto, Y.; Kitazumi, Y.; Shirai, O.; Yamamoto, M.; Kano, K.
Role of 2-mercaptoethanol in direct electron transfer-type bioelectrocatalysis of fructose dehydrogenase at Au electrodes
Electrochim. Acta
170
242-247
2015
Gluconobacter sp.
-
brenda
Sugimoto, Y.; Kawai, S.; Kitazumi, Y.; Shirai, O.; Kano, K.
Function of C-terminal hydrophobic region in fructose dehydrogenase
Electrochim. Acta
176
976-981
2015
Gluconobacter oxydans, Gluconobacter oxydans 621H
-
brenda
Kawai, S.; Kitazumi, Y.; Shirai, O.; Kano, K.
Bioelectrochemical characterization of the reconstruction of heterotrimeric fructose dehydrogenase from its subunits
Electrochim. Acta
210
689-694
2016
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
Xia, H.; Hibino, Y.; Kitazumi, Y.; Shirai, O.; Kano, K.
Interaction between D-fructose dehydrogenase and methoxy-substituent-functionalized carbon surface to increase productive orientations
Electrochim. Acta
218
41-46
2016
Gluconobacter japonicus, Gluconobacter japonicus NBRC3260
-
brenda
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