74
3 Fundamentals of DET-Type Bioelectrocatalysis
The half-wave potential of the sigmoidal part without the residual slope is almost
identical with E
o
E when the response is Nernstian, or the sigmoidal part gives kinetic
information on the heterogeneous electron transfer of the enzymes with suitable
orientations. Practically, we can consider a virtual current–potential linear line with
a slope that is identical to the residual slope and going through the onset position of
the DET-type wave (that is, almost identical with the dotted line in Fig. 3.5). The
current due to the virtual linear voltammogram is subtracted from the experimental
data (that corresponds to the solid line in Fig. 3.5) to give a sigmoidal wave (that is
almost identical to the dot-dashed line in Fig. 3.5). An example of successful analyses
was reported for W-containing FoDH [7].
As described in this section, rather quantitative analysis has been realized for the
steady-state waves of DET-type bioelectrocatalysis. The analysis is very important,
not only for proper understanding of the reaction and improvement of the reaction system, but also for thermodynamic and kinetic analyses of the enzyme. The
electrochemical information to be obtained is very useful in the field of biochemistry.
References
1. Armstrong FA, Hill HAO, Walton NJ (1988) Direct electrochemistry of redox proteins. Acc
Chem Res 21:407–413
2. Barker PD, Hill HAO (1988) Direct electrochemical probes of redox protein and redox enzyme
structure and functions. In: King TE, Mason HS, Morrison M (eds) Oxidases and related redox
systems. Alan R. Liss Inc., New York
3. Frew JE, Hill HAO (1988) Direct and indirect electron-transfer between electrodes and redox
proteins. Eur J Biochem 172:261–269
4. Frew JE, Hill HAO, Thomas JDR (1987) Electron-transfer Biosensor. Phil Trans R Soc London
316:95–106
5. Armstrong FA, Hill HAO, Oliver BN, Whitford D (1985) Direct electrochemistry of the photosynthetic blue copper protein plastocyanin-electrostatic promotion of rapid charge-transfer at
an edge-oriented pyrolytic graphite electrode. J Am Chem Soc 107:1473–1476
6. Berezin IV, Bogdanovskaya VA, Varfolomeev SD, Tarasevich MR, Iaropolov AI (1978)
Bioelectrocatalysis-equilibrium oxygen potential in presence of laccase. Dokl Akad Nauk
SSSR 240:615–618 (In Russian)
7. Lee CW, Gray HB, Anson FC, Malmström BG (1984) Catalysis of the reduction of dioxygen
at graphite electrodes coated with fungal laccase A. J Electroanal Chem 172:289–300
8. Guo LH, Hill HAO, Lawrance GA, Sanghera GS, Hopper DJ (1989) Direct un-mediated
electrochemistry of the enzyme p-cresolmethylhydroxylase. J Electroanal Chem 266:379–396
9. Burrows AL, Hill HAO, Leese TA, McIntire WS, Nakayama H, Sanghera GS (1991) Direct
electrochemistry of the enzyme, methylamine dehydrogenase from bacterium W3A1. Eur J
Biochem 199:73–78
10. Ikeda T, Fushimi F, Miki K, Senda M (1988) Direct bioelectrocatalysis at electrodes modified
D-gluconate dehydrogenase. Agric Biol Chem 52:2655–2658
11. Ikeda T, Matsushita F, Senda M (1991) Amperometric fructose sensor based on direct
bioelectrocatalysis. Biosens Bioelectron 6:299–304
12. Ikeda T, Miyaoka S, Matsushita F, Kobayashi D, Senda M (1992) Direct bioelectrocatalysis at
metal and carbon electrodes modified with adsorbed D-gluconate dehydrogenase or adsorbed
alcohol dehydrogenase. Chem Lett 21:847–850
3 Fundamentals of DET-Type Bioelectrocatalysis
The half-wave potential of the sigmoidal part without the residual slope is almost
identical with E
o
E when the response is Nernstian, or the sigmoidal part gives kinetic
information on the heterogeneous electron transfer of the enzymes with suitable
orientations. Practically, we can consider a virtual current–potential linear line with
a slope that is identical to the residual slope and going through the onset position of
the DET-type wave (that is, almost identical with the dotted line in Fig. 3.5). The
current due to the virtual linear voltammogram is subtracted from the experimental
data (that corresponds to the solid line in Fig. 3.5) to give a sigmoidal wave (that is
almost identical to the dot-dashed line in Fig. 3.5). An example of successful analyses
was reported for W-containing FoDH [7].
As described in this section, rather quantitative analysis has been realized for the
steady-state waves of DET-type bioelectrocatalysis. The analysis is very important,
not only for proper understanding of the reaction and improvement of the reaction system, but also for thermodynamic and kinetic analyses of the enzyme. The
electrochemical information to be obtained is very useful in the field of biochemistry.
References
1. Armstrong FA, Hill HAO, Walton NJ (1988) Direct electrochemistry of redox proteins. Acc
Chem Res 21:407–413
2. Barker PD, Hill HAO (1988) Direct electrochemical probes of redox protein and redox enzyme
structure and functions. In: King TE, Mason HS, Morrison M (eds) Oxidases and related redox
systems. Alan R. Liss Inc., New York
3. Frew JE, Hill HAO (1988) Direct and indirect electron-transfer between electrodes and redox
proteins. Eur J Biochem 172:261–269
4. Frew JE, Hill HAO, Thomas JDR (1987) Electron-transfer Biosensor. Phil Trans R Soc London
316:95–106
5. Armstrong FA, Hill HAO, Oliver BN, Whitford D (1985) Direct electrochemistry of the photosynthetic blue copper protein plastocyanin-electrostatic promotion of rapid charge-transfer at
an edge-oriented pyrolytic graphite electrode. J Am Chem Soc 107:1473–1476
6. Berezin IV, Bogdanovskaya VA, Varfolomeev SD, Tarasevich MR, Iaropolov AI (1978)
Bioelectrocatalysis-equilibrium oxygen potential in presence of laccase. Dokl Akad Nauk
SSSR 240:615–618 (In Russian)
7. Lee CW, Gray HB, Anson FC, Malmström BG (1984) Catalysis of the reduction of dioxygen
at graphite electrodes coated with fungal laccase A. J Electroanal Chem 172:289–300
8. Guo LH, Hill HAO, Lawrance GA, Sanghera GS, Hopper DJ (1989) Direct un-mediated
electrochemistry of the enzyme p-cresolmethylhydroxylase. J Electroanal Chem 266:379–396
9. Burrows AL, Hill HAO, Leese TA, McIntire WS, Nakayama H, Sanghera GS (1991) Direct
electrochemistry of the enzyme, methylamine dehydrogenase from bacterium W3A1. Eur J
Biochem 199:73–78
10. Ikeda T, Fushimi F, Miki K, Senda M (1988) Direct bioelectrocatalysis at electrodes modified
D-gluconate dehydrogenase. Agric Biol Chem 52:2655–2658
11. Ikeda T, Matsushita F, Senda M (1991) Amperometric fructose sensor based on direct
bioelectrocatalysis. Biosens Bioelectron 6:299–304
12. Ikeda T, Miyaoka S, Matsushita F, Kobayashi D, Senda M (1992) Direct bioelectrocatalysis at
metal and carbon electrodes modified with adsorbed D-gluconate dehydrogenase or adsorbed
alcohol dehydrogenase. Chem Lett 21:847–850