References
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49. Flexer V, Durand F, Tsujimura S, Mano N (2011) Efficient direct electron transfer of PQQglucose dehydrogenase on carbon cryogel electrodes at neutral pH. Anal Chem 83:5721–5727
50. Kielb P, Sezer M, Katz S, Lopez F, Schulz C, Gorton L, Ludwig R, Wollenberer U, Zebger I,
Weidinger IM (2015) Spectroscopic observation of calcium-nduced reorientation of cellobiose
dehydrogenase activity. ChemPhysChem 16:1960–1968
51. Ivnitski D, Atanassov P, Apblett C (2007) Direct bioelectrocatalysis of PQQ-dependent glucose
dehydrogenase. Electroanalysis 19:1562–1568
52. Wilson GS (2016) Native glucose oxidase does not undergo direct electron transfer. Biosens
Bioelectron 82:vii–viii
53. Bartlett PN, Al-Lolage FA (2018) There is no evidence to support literature claims of direct
electron transfer (DET) for native glucose oxidase (GOx) at carbon nanotubes or graphene. J
Electroanal Chem 819:26–37
54. Sakai K, Sugimoto Y, Kitazumi Y, Shirai O, Takagi K, Kano K (2017) Direct electron transfertype bioelectrocatalytic interconversion of carbon dioxide/formate and NAD + /NADH redox
couples with Tungsten-containing formate dehydrogenase. Electrochim Acta 228:537–544
55. Sato A, Takagi K, Kano K, Kato N, Duine JA, Ikeda T (2001) Ca 2+ stabilizes the semiquinone
radical of pyrroloquinoline quinone. Biochem J 357:893–898
56. Yehezkeli O, Raichlin S, Tel-Vered R, Kesselman E, Danino D, Willner I (2010) Biocatalytic
implant of Pt nanoclusters into glucose oxidase: a method to electrically wire the enzyme and
to transform it from an oxidase to a hydrogenase. J Phys Chem Lett 1:2816–2819
57. Trifonov A, Stemmer A, Tel-Vered R (2019) Enzymatically self-wiring in nanopores and its
application in direct electron transfer biofuel cells. Nanoscale Adv 1:347–356
58. Muguruma H, Iwasa H, Hidaka H, Hiratsuka A, Uzawa H (2016) Mediatorless direct electron
transfer between flavin adenine dinucleotide-dependent glucose dehydrogenase and singlewalled carbon nanotubes. ACS Catal 7:725–734
59. Adachi T, Fujii T, Honda M, Kitazumi Y, Shirai O, Kano K (2020) Direct electron transfer-type
bioelectrocatalysis of FAD-dependent glucose dehydrogenase using porous gold electrodes and
enzymatically implanted platinum nanoclusters. Bioelectrochemistry 133:107457
60. He B, Sinclair R, Copeland BR, Makino R, Powers LS, Yamazaki I (1996) The
structure−function relationship and reduction potentials of high oxidation states of myoglobin
and peroxidase. Biochemistry 25:2413–2420
61. Farhangrazi ZS, Fossett ME, Powers LS, Ellis Jr WR (1995) Variable-temperature spectroelectrochemical study of horseradish peroxidase. Biochemistry 34:2866–2871
62. Jönsson G, Gorton L (1989) An electrochemical sensor for hydrogen peroxide based on
peroxidase adsorbed on a spectrographic graphite electrode. Electroanalysis 5:465–468
63. Bogdanovskay VA, Fridman VA, Tarasevich MR, Scheller F (1994) Bioelectrocatalysis by
immobilized peroxidase: the reaction mechanism and the possibility of electroanalytical
detection of both inhibitors and activators of enzyme. Anal Lett 27:2823–2847
64. Ferapontova EE, Gorton L (2001) Effect of proton donors on direct electron transfer in the
system gold electrode-horseradish peroxidase. Electrochem Commun 3:767–774
65. Ferapontova E, Puganova E (2002) Effect of pH on direct electron transfer between graphite
and horseradish peroxidase. J Electroanal Chem 51:20–26
66. Ferapontova E (2004) Direct peroxidase bioelectrocatalysis on a variety of electrode materials.
Electroanalysis 16:1101–1112
67. 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
68. Marcus RA (1964) Chemical and electrochemical electron-transfer theory. Annu Rev Phys
Chem 15:155–156
69. Marcus RA (1993) Electron transfer reactions in chemistry: theory and experiment (nobel
lecture). Angew Chem Int Ed 32:1111–1121
70. Gray HB, Winkler JR (2005) Long-range electron transfer. Proc Natl Acad Sci USA 102:3534–
3539
77
49. Flexer V, Durand F, Tsujimura S, Mano N (2011) Efficient direct electron transfer of PQQglucose dehydrogenase on carbon cryogel electrodes at neutral pH. Anal Chem 83:5721–5727
50. Kielb P, Sezer M, Katz S, Lopez F, Schulz C, Gorton L, Ludwig R, Wollenberer U, Zebger I,
Weidinger IM (2015) Spectroscopic observation of calcium-nduced reorientation of cellobiose
dehydrogenase activity. ChemPhysChem 16:1960–1968
51. Ivnitski D, Atanassov P, Apblett C (2007) Direct bioelectrocatalysis of PQQ-dependent glucose
dehydrogenase. Electroanalysis 19:1562–1568
52. Wilson GS (2016) Native glucose oxidase does not undergo direct electron transfer. Biosens
Bioelectron 82:vii–viii
53. Bartlett PN, Al-Lolage FA (2018) There is no evidence to support literature claims of direct
electron transfer (DET) for native glucose oxidase (GOx) at carbon nanotubes or graphene. J
Electroanal Chem 819:26–37
54. Sakai K, Sugimoto Y, Kitazumi Y, Shirai O, Takagi K, Kano K (2017) Direct electron transfertype bioelectrocatalytic interconversion of carbon dioxide/formate and NAD + /NADH redox
couples with Tungsten-containing formate dehydrogenase. Electrochim Acta 228:537–544
55. Sato A, Takagi K, Kano K, Kato N, Duine JA, Ikeda T (2001) Ca 2+ stabilizes the semiquinone
radical of pyrroloquinoline quinone. Biochem J 357:893–898
56. Yehezkeli O, Raichlin S, Tel-Vered R, Kesselman E, Danino D, Willner I (2010) Biocatalytic
implant of Pt nanoclusters into glucose oxidase: a method to electrically wire the enzyme and
to transform it from an oxidase to a hydrogenase. J Phys Chem Lett 1:2816–2819
57. Trifonov A, Stemmer A, Tel-Vered R (2019) Enzymatically self-wiring in nanopores and its
application in direct electron transfer biofuel cells. Nanoscale Adv 1:347–356
58. Muguruma H, Iwasa H, Hidaka H, Hiratsuka A, Uzawa H (2016) Mediatorless direct electron
transfer between flavin adenine dinucleotide-dependent glucose dehydrogenase and singlewalled carbon nanotubes. ACS Catal 7:725–734
59. Adachi T, Fujii T, Honda M, Kitazumi Y, Shirai O, Kano K (2020) Direct electron transfer-type
bioelectrocatalysis of FAD-dependent glucose dehydrogenase using porous gold electrodes and
enzymatically implanted platinum nanoclusters. Bioelectrochemistry 133:107457
60. He B, Sinclair R, Copeland BR, Makino R, Powers LS, Yamazaki I (1996) The
structure−function relationship and reduction potentials of high oxidation states of myoglobin
and peroxidase. Biochemistry 25:2413–2420
61. Farhangrazi ZS, Fossett ME, Powers LS, Ellis Jr WR (1995) Variable-temperature spectroelectrochemical study of horseradish peroxidase. Biochemistry 34:2866–2871
62. Jönsson G, Gorton L (1989) An electrochemical sensor for hydrogen peroxide based on
peroxidase adsorbed on a spectrographic graphite electrode. Electroanalysis 5:465–468
63. Bogdanovskay VA, Fridman VA, Tarasevich MR, Scheller F (1994) Bioelectrocatalysis by
immobilized peroxidase: the reaction mechanism and the possibility of electroanalytical
detection of both inhibitors and activators of enzyme. Anal Lett 27:2823–2847
64. Ferapontova EE, Gorton L (2001) Effect of proton donors on direct electron transfer in the
system gold electrode-horseradish peroxidase. Electrochem Commun 3:767–774
65. Ferapontova E, Puganova E (2002) Effect of pH on direct electron transfer between graphite
and horseradish peroxidase. J Electroanal Chem 51:20–26
66. Ferapontova E (2004) Direct peroxidase bioelectrocatalysis on a variety of electrode materials.
Electroanalysis 16:1101–1112
67. 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
68. Marcus RA (1964) Chemical and electrochemical electron-transfer theory. Annu Rev Phys
Chem 15:155–156
69. Marcus RA (1993) Electron transfer reactions in chemistry: theory and experiment (nobel
lecture). Angew Chem Int Ed 32:1111–1121
70. Gray HB, Winkler JR (2005) Long-range electron transfer. Proc Natl Acad Sci USA 102:3534–
3539
