78
3 Fundamentals of DET-Type Bioelectrocatalysis
71. Moser CC, Keske JM, Warncke K, Farid RS, Dutton PL (1992) Nature of biological electron
transfer. Nature 355:796–802
72. Léger C, Jones AK, Albracht SPJ, Armstrong FA (2002) Effect of a dispersion of interfacial
electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and
other enzymes. J Phys Chem B 106:13058–13063
73. Léger C, Bertrand P (2008) Direct electrochemistry of redox enzymes as tool for mechanistic
studies. Chem Rev 108:2379–2438
74. Sugimoto Y, Takeuchi R, Kitazumi Y, Shirai O, Kano K (2016) Significance of mesoporous
electrodes for noncatalytic faradaic process of randomly oriented redox proteins. J Phys Chem
C 120:26270–26277
75. Sensi M, del Barrio M, Baffert C, Fourmond V, Léger C (2017) New perspectives in hydrogenase
direct electrochemistry. Curr Opin Electrochem 5:135–145
76. Xia H-Q, Kitazumi Y, Shirai O, Kano K (2016) Enhanced direct electron transfer-type bioelectrocatalysis of bilirubin oxidase on negatively charged aromatic compound-modified carbon
electrode. J Electroanal Chem 763:104–109
77. Xia H-Q, Hibino Y, Kitazumi Y, Shirai O, Kano K (2016) Interaction between d-fructose
dehydrogenase and methoxy-substituent-functionalized carbon surface to increase productive
orientations. Electrochim Acta 218:41–46
78. Kaida Y, Hibino Y, Kitazumi Y, Shirai O, Kano K (2019) Ultimate downsizing of Dfructose dehydrogenase for improving the performance of direct electron transfer-type
bioelectrocatalysis. Electrochem Commun 98:101–105
79. Takahashi Y, Kitazumi Y, Shirai O, Kano K (2019) Improved Direct electron transfer-type
bioelectrocatalysis of bilirubin oxidase using thiol-modified gold nanoparticles on mesoporous
carbon electrode. J Electroanal Chem 832:158–164
80. So K, Kitazumi Y, Shirai O, Kurita K, Nishihara H, Higuchi Y, Kano K (2014) Kinetic analysis
of inactivation and enzyme reaction of oxygen-tolerant [NiFe]-hydrogenase at direct electrontransfer bioanode. Bull. Chem. Soc. Jpn. 87:1177–1185
3 Fundamentals of DET-Type Bioelectrocatalysis
71. Moser CC, Keske JM, Warncke K, Farid RS, Dutton PL (1992) Nature of biological electron
transfer. Nature 355:796–802
72. Léger C, Jones AK, Albracht SPJ, Armstrong FA (2002) Effect of a dispersion of interfacial
electron transfer rates on steady state catalytic electron transport in [NiFe]-hydrogenase and
other enzymes. J Phys Chem B 106:13058–13063
73. Léger C, Bertrand P (2008) Direct electrochemistry of redox enzymes as tool for mechanistic
studies. Chem Rev 108:2379–2438
74. Sugimoto Y, Takeuchi R, Kitazumi Y, Shirai O, Kano K (2016) Significance of mesoporous
electrodes for noncatalytic faradaic process of randomly oriented redox proteins. J Phys Chem
C 120:26270–26277
75. Sensi M, del Barrio M, Baffert C, Fourmond V, Léger C (2017) New perspectives in hydrogenase
direct electrochemistry. Curr Opin Electrochem 5:135–145
76. Xia H-Q, Kitazumi Y, Shirai O, Kano K (2016) Enhanced direct electron transfer-type bioelectrocatalysis of bilirubin oxidase on negatively charged aromatic compound-modified carbon
electrode. J Electroanal Chem 763:104–109
77. Xia H-Q, Hibino Y, Kitazumi Y, Shirai O, Kano K (2016) Interaction between d-fructose
dehydrogenase and methoxy-substituent-functionalized carbon surface to increase productive
orientations. Electrochim Acta 218:41–46
78. Kaida Y, Hibino Y, Kitazumi Y, Shirai O, Kano K (2019) Ultimate downsizing of Dfructose dehydrogenase for improving the performance of direct electron transfer-type
bioelectrocatalysis. Electrochem Commun 98:101–105
79. Takahashi Y, Kitazumi Y, Shirai O, Kano K (2019) Improved Direct electron transfer-type
bioelectrocatalysis of bilirubin oxidase using thiol-modified gold nanoparticles on mesoporous
carbon electrode. J Electroanal Chem 832:158–164
80. So K, Kitazumi Y, Shirai O, Kurita K, Nishihara H, Higuchi Y, Kano K (2014) Kinetic analysis
of inactivation and enzyme reaction of oxygen-tolerant [NiFe]-hydrogenase at direct electrontransfer bioanode. Bull. Chem. Soc. Jpn. 87:1177–1185