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Ligand ferricenium ion

Basic Ligand Information

Molecular Structure

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (14 results)

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Show Natural Substrate (14 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.99.29

cellobiose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-fructose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-galactose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-glucose + ferricenium ion = 3-dehydro-D-glucose + ferrocene

724043

-

1.1.99.29

D-maltose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-mannose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-ribose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-talose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-xylose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

L-arabinose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

L-sorbose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

lactose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

maltotriose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

xylobiose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

14 entries

Substrate in Enzyme-catalyzed Reactions (40 results)

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Show Substrate (40 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

1.1.3.10

D-galactose + ferricenium ion = 2-dehydro-D-galactose + ferrocenium ion

697917

-

1.1.3.10

D-glucose + ferricenium ion = 2-dehydro-D-glucose + ferrocenium ion

697917, 741294

-

1.1.5.9

D-glucose + ferricenium ion = D-glucono-1,5-lactone + ferrocenium ion

725879

-

1.1.5.9

D-xylose + ferricenium ion = D-xylono-1,5-lactone + ferrocenium ion

723928, 725879

-

1.1.3.10

2 entries

1.1.5.9

2 entries

1.1.99.18

lactose + ferricenium ion = 4-O-(beta-D-galactopyranosyl)-D-glucono-1,5-lactone + ?

654308

-

1.1.99.29

2-deoxy-D-glucose + ferricenium ion = ?

644547

-

1.1.99.29

cellobiose + ferricenium ion = ?

644547

-

1.1.99.29

cellobiose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-allose + ferricenium ion = ? + ferrocene

739926

-

1.1.99.29

D-fructose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-galactose + ferricenium ion = ?

644547

-

1.1.99.29

D-galactose + ferricenium ion = ? + ferrocene

710969, 739926, 724043

-

1.1.99.29

D-glucono-1,5-lactone + ferricenium ion = ?

644547

-

1.1.99.29

D-glucose + ferricenium ion = 2-dehydro-D-glucose + ferrocene

741112, 739926

-

1.1.99.29

D-glucose + ferricenium ion = 3-dehydro-D-glucose + ferrocene

710969, 724043, 644547

-

1.1.99.29

D-lyxose + ferricenium ion = ?

644547

-

1.1.99.29

D-maltose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-mannose + ferricenium ion = ?

644547

-

1.1.99.29

D-mannose + ferricenium ion = ? + ferrocene

724043, 739926

-

1.1.99.29

D-ribose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-talose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

D-xylobiose + ferricenium ion = ?

687883

-

1.1.99.29

D-xylose + ferricenium ion = ?

644547

-

1.1.99.29

D-xylose + ferricenium ion = ? + ferrocene

710969, 724043, 739926

-

1.1.99.29

L-arabinose + ferricenium ion = ?

644547

-

1.1.99.29

L-arabinose + ferricenium ion = ? + ferrocene

710969, 724043

-

1.1.99.29

L-glucose + ferricenium ion = ?

644547

-

1.1.99.29

L-sorbose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

lactose + ferricenium ion = ? + ferrocene

739926, 710969, 724043

-

1.1.99.29

maltose + ferricenium ion = ?

644547

-

1.1.99.29

maltose + ferricenium ion = ? + ferrocene

739926

-

1.1.99.29

maltotriose + ferricenium ion = ?

644547, 687883

-

1.1.99.29

maltotriose + ferricenium ion = ? + ferrocene

724043, 739926

-

1.1.99.29

methyl-alpha-D-galactopyranoside + ferricenium ion = ?

644547

-

1.1.99.29

methyl-alpha-D-glucopyranoside + ferricenium ion = ?

644547

-

1.1.99.29

methyl-alpha-D-glucopyranoside + ferricenium ion = ? + ferrocene

739926

-

1.1.99.29

methyl-beta-D-glucopyranoside + ferricenium ion = ?

644547

-

1.1.99.29

sucrose + ferricenium ion = ?

644547

-

1.1.99.29

trehalose + ferricenium ion = ?

644547

-

1.1.99.29

xylobiose + ferricenium ion = ? + ferrocene

724043

-

1.1.99.29

35 entries

Enzyme Kinetic Parameters

k_cat Value (Turnover Number) (25 results)

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Show Turnover Number (25 entries)

EC NUMBER

TURNOVER NUMBER [1/S]

TURNOVER NUMBER MAXIMUM [1/S]

COMMENTARY

LITERATURE

1.1.3.10

1.44

-

E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

1.81

-

L537G/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

2.08

-

E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

2.11

-

L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

2.47

-

L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

2.68

-

L537W/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

5.34

-

wild-type, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

7.07

-

L537G mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

8.18

-

L537W mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

46.7

-

E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

54.4

-

E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

86.3

-

L537W/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

86.7

-

L537G/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

102

-

L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

127

-

L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

151

-

wild-type, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

282

-

L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

334

-

L537W mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.99.18

34.7

-

pH 4.5, 30°C, reaction with lactose

654308

1.1.99.18

35.6

-

pH 4.5, 30°C, reaction with lactose

654308

1.1.99.29

9.86

-

isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C

739926

1.1.99.29

48.1

-

isoform PDH2, at pH 8.5 and 30°C

739926

1.1.99.29

104

-

native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5

710969

1.1.99.29

130

-

isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C

739926

1.1.99.29

203

-

recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5

710969

1.1.3.10

18 entries

1.1.99.18

2 entries

1.1.99.29

5 entries

K_M Value (43 results)

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Show KM Value (43 entries)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

1.1.3.10

0.054

-

L537G/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.054

-

mutant enzyme L537G/E542R, at pH 6.5 and 30°C

697917

1.1.3.10

0.063

-

L537W mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.063

-

mutant enzyme L537W, at pH 6.5 and °C

697917

1.1.3.10

0.068

-

E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.068

-

mutant enzyme E542K, at pH 6.5 and 30°C

697917

1.1.3.10

0.07

-

wild type enzyme, at pH 6.5 and 30°C

697917

1.1.3.10

0.07

-

wild-type, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.072

-

L537G/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.072

-

mutant enzyme L537G/E542K, at pH 6.5 and 30°C

697917

1.1.3.10

0.074

-

L537W/E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.074

-

mutant enzyme L537W/E542R, at pH 6.5 and 30°C

697917

1.1.3.10

0.086

-

L537G mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.086

-

mutant enzyme L537G, at pH 6.5 and 30°C

697917

1.1.3.10

0.09

-

L537W/E542K mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.09

-

mutant enzyme L537W/E542K, at pH 6.5 and 30°C

697917

1.1.3.10

0.183

-

E542R mutant, substrate ferricenium ion (D-galactose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.183

-

mutant enzyme E542R, at pH 6.5 and 30°C

697917

1.1.3.10

0.253

-

L537W mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.253

-

mutant enzyme L537W, at pH 6.5 and 30°C

697917

1.1.3.10

0.254

-

wild type enzyme, at pH 6.5 and 30°C

697917

1.1.3.10

0.254

-

wild-type, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.281

-

L537W/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.281

-

mutant enzyme L537W/E542R, at pH 6.5 and 30°C

697917

1.1.3.10

0.289

-

L537G mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.289

-

mutant enzyme L537G, at pH 6.5 and 30°C

697917

1.1.3.10

0.29

-

E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.29

-

mutant enzyme E542K, at pH 6.5 and 30°C

697917

1.1.3.10

0.296

-

L537G/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.296

-

mutant enzyme L537G/E542K, at pH 6.5 and 30°C

697917

1.1.3.10

0.319

-

E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.319

-

mutant enzyme E542R, at pH 6.5 and 30°C

697917

1.1.3.10

0.328

-

L537G/E542R mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.328

-

mutant enzyme L537G/E542K, at pH 6.5 and 30°C

697917

1.1.3.10

0.408

-

L537W/E542K mutant, substrate ferricenium ion (D-glucose concentration constant, 100 mM), standard chromogenic ABTS assay (azino-bis-(3-ethylbenzthiazolin-6-sulfonic acid), horse-radish peroxidase, measuring absorbtion at 420 nm), pH 6.5, 30°C

697917

1.1.3.10

0.408

-

mutant enzyme L537W/E542K, at pH 6.5 and 30°C

697917

1.1.99.18

0.00099

-

pH 4.5, 30°C, reaction with lactose

654308

1.1.99.18

0.0012

-

pH 4.5, 30°C, reaction with lactose

654308

1.1.99.29

0.0103

-

isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C

739926

1.1.99.29

0.0201

-

isoform PDH2, at pH 8.5 and 30°C

739926

1.1.99.29

0.13

-

native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5

710969

1.1.99.29

0.161

-

isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C

739926

1.1.99.29

0.22

-

recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 8.5

710969

1.1.3.10

36 entries

1.1.99.18

2 entries

1.1.99.29

5 entries

References & Links

Literature References (11)

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Show Reference (11 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

644547

11511865

Screening of basidiomycete fungi for the quinone-dependent sugar C-2/C-3 oxidoreductase, pyranose dehydrogenase, and properties of the enzyme from Macrolepiota rhacodes

2001

Volc, J.; Kubátová, E.; Daniel, G.; Sedmera, P.; Haltrich, D.

Arch. Microbiol.

176

178-186

654308

14666391

Characterization of cellobiose dehydrogenase from the white rot fungi Trametes pubescens and Trametes villosa

2004

Ludwig, R.; Salamon, A.; Varga, J.; Zamocky, M.; Peterbauer, C.K.; Kulbe, K.D.; Haltrich, D.

Appl. Microbiol. Biotechnol.

64

213-222

687883

18083263

Characterization of pyranose dehydrogenase from Agaricus meleagris and its application in the C-2 specific conversion of D-galactose

2008

Sygmund, C.; Kittl, R.; Volc, J.; Halada, P.; Kubatova, E.; Haltrich, D.; Peterbauer, C.K.

J. Biotechnol.

133

334-342

697917

19143837

Improving thermostability and catalytic activity of pyranose 2-oxidase from Trametes multicolor by rational and semi-rational design

2009

Spadiut, O.; Leitner, C.; Salaheddin, C.; Varga, B.; Vertessy, B.G.; Tan, T.C.; Divne, C.; Haltrich, D.

FEBS J.

276

776-792

710969

19888575

Heterologous expression of an Agaricus meleagris pyranose dehydrogenase-encoding gene in Aspergillus spp. and characterization of the recombinant enzyme

2010

Pisanelli, I.; Kujawa, M.; Gschnitzer, D.; Spadiut, O.; Seiboth, B.; Peterbauer, C.

Appl. Microbiol. Biotechnol.

86

599-606

723928

22222911

Characterization of different FAD-dependent glucose dehydrogenases for possible use in glucose-based biosensors and biofuel cells

2012

Zafar, M.N.; Beden, N.; Leech, D.; Sygmund, C.; Ludwig, R.; Gorton, L.

Anal. Bioanal. Chem.

402

2069-2077

724043

19768457

Pyranose dehydrogenases: Biochemical features and perspectives of technological applications

2010

Peterbauer, C.; Volc, J.

Appl. Microbiol. Biotechnol.

85

837-848

725879

22151971

Heterologous overexpression of Glomerella cingulata FAD-dependent glucose dehydrogenase in Escherichia coli and Pichia pastoris

2011

Sygmund, C.; Staudigl, P.; Klausberger, M.; Pinotsis, N.; Djinovic-Carugo, K.; Gorton, L.; Haltrich, D.; Ludwig, R.

Microb. Cell Fact.

10

106

739926

27995309

Characterization of three pyranose dehydrogenase isoforms from the litter-decomposing basidiomycete Leucoagaricus meleagris (syn. Agaricus meleagris)

2017

Graf, M.M.; Weber, S.; Kracher, D.; Kittl, R.; Sygmund, C.; Ludwig, R.; Peterbauer, C.; Haltrich, D.

Appl. Microbiol. Biotechnol.

101

2879-2891

741112

25752794

Engineering of pyranose dehydrogenase for application to enzymatic anodes in biofuel cells

2015

Yakovleva, M.E.; Gonaus, C.; Schropp, K.; OConghaile, P.; Leech, D.; Peterbauer, C.K.; Gorton, L.

Phys. Chem. Chem. Phys.

17

9074-9081

741294

25296188

Engineering pyranose 2-oxidase for modified oxygen reactivity

2014

Brugger, D.; Krondorfer, I.; Shelswell, C.; Huber-Dittes, B.; Haltrich, D.; Peterbauer, C.K.

PLoS ONE

9

e109242

Links to other databases for ferricenium ion

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ChEBI

PubChem

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