3.1 History of DET-Type Bioelectrocatalysis
63
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
Glucose dehydrogenase
(Burkholderia cepacia)
FAD (covalent), 3Fe3S,
heme c(proximal),
heme c(medial),
heme c(distal)
[heterotrimer]
glucose – 2e −
(?) Carbon screen-printed
electrodes
[38] 2y0e
Fructose dehydrogenase
(Gluconobacter japonicus)
FAD (covalent), heme c
(proximal), heme c
(medial), heme c
(distal) [heterotrimer]
fructose – 2e −
(0.08 V vs.
Ag|AgCl, pH 5)
KBE
[39]
fructose – 2e −
(0.25 V vs.
Ag|AgCl, pH 5)
Mercaptoetanol-modified
AuNP
[40]
Nitrate reductase (Neurospora
crassa)
(Mo-pterin, heme, FAD)×2 [homodimer]
NO
3
−
+ 2e −
(−0.15 V vs.
SHE, pH 7)
PEI-PM/EPGE
[41]
Gluconate 2-dehydrogenase
(Gluconobacter frateurii)
FAD (covalent), (heme c)×2
[heterotrimer]
gluconate – 2e −
(0.1 V vs.
Ag|AgCl, pH 5)
ITO
[42]
p-cresolmethyhydroxylase
(Pseudomonas putlda)
(FAD, heme)×2 [a
2 b
2 heterotetramer]
p-cresol
– 2e −
(0 V vs. SCE, pH
7)
Cu(NH
3 )
6
3+
(promoter)/EPGE [8]
Quinohemoprotein
Glucose dehydrogenase
(Ewingella americana)
PQQ (non-covalent), heme c
[monomer]
glucose – 2e −
(−0.1 V vs. SCE,
pH 7)
4-aminothiophenol-modified
AuNP
[43]
Alcohol dehydrogenase
(Pseudomonas putida
HK5)
PQQ (non-covalent), heme c
[monomer]
glycerol – 4e −
(−0.1 V vs. SCE,
pH 7)
4-aminothiophenol-modified
AuNP
[44] 1KV9
(continued)