4.5 DET-Type Bi-Way Bioelectrocatalysis
89
In addition, considering the fact that E i = 0 value of the bi-directional
catalytic wave corresponds to the E eq value of the substrates (CO 2 /HCOO
− and
NAD
+ /NADH), the standard rate constant of the interfacial electron transfer between
the electron-donating/accepting site (FeS cluster) in FoDH and the mesoporous
electrode is quite large when the enzyme is adsorbed in productive orientations.
References
1. de Poulpiquet A, Ciaccafava A, Lojou E (2014) New trends in enzyme immobilization
at nanostructured interfaces for efficient electrocatalysis in biofuel cells. Electrochim Acta
126:104–114
2. Tsutsumi M, Tsujimura S, Shirai O, Kano K (2009) Direct electrochemistry of histamine
dehydrogenase from Nocardioides simplex. J Electroanal Chem 625:144–148
3. Murata K, Suzuki M, Kajiya K, Nakamura K, Ohno H (2009) High performance bioanode based
on direct electron transfer of fructose dehydrogenase at gold nanoparticle-modified electrodes.
Electrochem Commun 11:668–671
4. Siepenkoetter T, Salaj-Kosla U, Magner E (2017) The immobilization of fructose dehydrogenase on nanoporous gold electrodes for the detection of fructose. ChemElectroChem
4:905–912
5. Bollella P, Hibino Y, Kano K, Gorton L, Antiochia R (2018) Highly sensitive membraneless
fructose biosensor based on fructose dehydrogenase immobilized onto aryl thiol modified
highly porous gold electrode: characterization and application in food samples. Anal Chem
90:12131–12136
6. Tsujimura S, Nishina A, Hamano Y, Kano K, Shiraishi S (2010) Electrochemical reaction of
fructose dehydrogenase on carbon cryogel electrodes with controlled pore sizes. J Electroanal
Chem 12:446–449
7. Funabashi H, Takeuchi S, Tsujimura S (2017) Hierarchical meso/macro-porous carbon fabricated from dual MgO templates for direct electron transfer enzymatic electrodes. Sci Rep
7:45147
8. Sakai K, Kitazumi Y, Shirai O, Kano K (2018) Nanostructured porous electrodes by the anodization of gold for an application as scaffolds in direct-electron-transfer-type bioelectrocatalysis.
Anal Sci 34:1317–1322
9. Xia H, Kitazumi Y, Shirai O, Kano K (2017) Direct electron transfer-type bioelectrocatalysis
of peroxidase at mesoporous carbon electrodes and its application for glucose determination
based on bienzyme system. Anal Sci 33:839–844
10. Sugimoto Y, Kitazumi Y, Shirai O, Kano K (2017) Effects of mesoporous structures on direct
electron transfer-type bioelectrocatalysis: facts and simulation on a three-dimensional model
of random orientation of enzymes. Electrochemistry 85:82–87
11. Kamitaka Y, Tsujimura S, Ikeda T, Kano K (2006) Electrochemical quartz crystal microbalance
study of direct bioelectrocatalytic reduction of bilirubin oxidase. Electrochemistry 74:642–644
12. Murata K, Kajiya K, Nakamura N, Ohno H (2009) Direct electrochemistry of bilirubin oxidase
on three-dimensional gold nanoparticle electrodes and its application in a biofuel cell. Energy
Environ Sci 2:1280–1285
13. Takahashi Y, Wanibuchi M, Kitazumi Y, Shirai O, Kano K (2019) Improved direct electron
transfer-type bioelectrocatalysis of bilirubin oxidase using porous gold electrodes. J Electroanal
Chem 843:47–53
14. Monsalve K, Roger M, Gutierrez-Sanchez C, Ilbert M, Nitsche S, Byrne-Kodjabachian D,
Marchi V, Lojou E (2015) Hydrogen bioelectrooxidation on gold nanoparticle-based electrodes
modified by Aquifex aeolicus hydrogenase: application to hydrogen/oxygen enzymatic biofuel
cells. Bioelectrochemistry 106:47–55
89
In addition, considering the fact that E i = 0 value of the bi-directional
catalytic wave corresponds to the E eq value of the substrates (CO 2 /HCOO
− and
NAD
+ /NADH), the standard rate constant of the interfacial electron transfer between
the electron-donating/accepting site (FeS cluster) in FoDH and the mesoporous
electrode is quite large when the enzyme is adsorbed in productive orientations.
References
1. de Poulpiquet A, Ciaccafava A, Lojou E (2014) New trends in enzyme immobilization
at nanostructured interfaces for efficient electrocatalysis in biofuel cells. Electrochim Acta
126:104–114
2. Tsutsumi M, Tsujimura S, Shirai O, Kano K (2009) Direct electrochemistry of histamine
dehydrogenase from Nocardioides simplex. J Electroanal Chem 625:144–148
3. Murata K, Suzuki M, Kajiya K, Nakamura K, Ohno H (2009) High performance bioanode based
on direct electron transfer of fructose dehydrogenase at gold nanoparticle-modified electrodes.
Electrochem Commun 11:668–671
4. Siepenkoetter T, Salaj-Kosla U, Magner E (2017) The immobilization of fructose dehydrogenase on nanoporous gold electrodes for the detection of fructose. ChemElectroChem
4:905–912
5. Bollella P, Hibino Y, Kano K, Gorton L, Antiochia R (2018) Highly sensitive membraneless
fructose biosensor based on fructose dehydrogenase immobilized onto aryl thiol modified
highly porous gold electrode: characterization and application in food samples. Anal Chem
90:12131–12136
6. Tsujimura S, Nishina A, Hamano Y, Kano K, Shiraishi S (2010) Electrochemical reaction of
fructose dehydrogenase on carbon cryogel electrodes with controlled pore sizes. J Electroanal
Chem 12:446–449
7. Funabashi H, Takeuchi S, Tsujimura S (2017) Hierarchical meso/macro-porous carbon fabricated from dual MgO templates for direct electron transfer enzymatic electrodes. Sci Rep
7:45147
8. Sakai K, Kitazumi Y, Shirai O, Kano K (2018) Nanostructured porous electrodes by the anodization of gold for an application as scaffolds in direct-electron-transfer-type bioelectrocatalysis.
Anal Sci 34:1317–1322
9. Xia H, Kitazumi Y, Shirai O, Kano K (2017) Direct electron transfer-type bioelectrocatalysis
of peroxidase at mesoporous carbon electrodes and its application for glucose determination
based on bienzyme system. Anal Sci 33:839–844
10. Sugimoto Y, Kitazumi Y, Shirai O, Kano K (2017) Effects of mesoporous structures on direct
electron transfer-type bioelectrocatalysis: facts and simulation on a three-dimensional model
of random orientation of enzymes. Electrochemistry 85:82–87
11. Kamitaka Y, Tsujimura S, Ikeda T, Kano K (2006) Electrochemical quartz crystal microbalance
study of direct bioelectrocatalytic reduction of bilirubin oxidase. Electrochemistry 74:642–644
12. Murata K, Kajiya K, Nakamura N, Ohno H (2009) Direct electrochemistry of bilirubin oxidase
on three-dimensional gold nanoparticle electrodes and its application in a biofuel cell. Energy
Environ Sci 2:1280–1285
13. Takahashi Y, Wanibuchi M, Kitazumi Y, Shirai O, Kano K (2019) Improved direct electron
transfer-type bioelectrocatalysis of bilirubin oxidase using porous gold electrodes. J Electroanal
Chem 843:47–53
14. Monsalve K, Roger M, Gutierrez-Sanchez C, Ilbert M, Nitsche S, Byrne-Kodjabachian D,
Marchi V, Lojou E (2015) Hydrogen bioelectrooxidation on gold nanoparticle-based electrodes
modified by Aquifex aeolicus hydrogenase: application to hydrogen/oxygen enzymatic biofuel
cells. Bioelectrochemistry 106:47–55