64
3 Fundamentals of DET-Type Bioelectrocatalysis
Table 3.1
(continued)
Enzyme group
Enzyme name (source)
Catalytic and redox center(s)* (subunit structure)
Reaction
(half-wave
potential of the
catalytic wave)
Electrode
Refs. PDB
Alcohol dehydrogenase
(Gluconobacter sp.)
PQQ (non-covalent), heme c,
heme c,
heme c,
heme c
[heterotrimer]
ethanol – 2e −
(0 V vs. Ag|AgCl,
pH 6)
polypyrrol-entrapped on Pt
[45]
Methylamine dehydrogenase
(bacterium W3A1)
(TTQ (covalent), heme c)×2
[a
2 b
2 heterotetramer]
RCH
2 NH2 – 2e −
(−0.15 V vs.
SCE, 7.2)
EPGE
[9]
Hemoprotein
Peroxidase (horseradish)
heme b
[monomer]
H
2 O
2 – 2e −
(0.6 V vs.
Ag|AgCl, pH 7)
KBE
[17] 1h58
Cytochrome c
peroxidase
(Nitrosomonas europaea)
heme c,
heme c
[monomer]
H
2 O
2 – 2e −
(0.5 V vs. SHE,
pH 7)
EPGE
[46] 1IQC
Cytochrome c
peroxidase (yeast) heme b
[monomer]
H
2 O
2 – 2e −
(0.65 V vs. SHE,
pH 7)
EPGE
[16]
Flavoprotein
Ferredoxin-NADP +
reductase
(Chlamydomonas reinhardtii)
FAD (non-covalent?) [monomer]
NADP +
+ 2e −
NADPH
(−0.35 V vs.
SHE, pH 8)
ITO/EPGE
[47] Reference
structure
1FNB
(spinachi)
1GAW
(cone)
Glucose oxidase (Aspergillus
niger)
FAD×2 (non-covalent) [homodimer]
glucose – 2e −
(−0.35 V vs.
Ag|AgCl, pH 7)
(?)
MWCNT/Pt
[48] 1CF3
Quinoprotein
(continued)