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72. Larsson T, Lindgren A, Ruzgas T (2001) Spectroelectrochemical study of cellobiose
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Bioelectrochemistry 53:243–249. https://doi.org/10.1016/S0302-4598(01)00099-X
73. Aguey-Zinsou KF, Bernhardt PV, Kappler U, McEwan AG (2003) Direct electrochemistry
of a bacterial sulfite dehydrogenase. J Am Chem Soc 125:530–535. https://doi.org/10.1021/
ja028293e
74. Christenson A, Gustavsson T, Gorton L, Hägerhäll C (2008) Direct and mediated electron
transfer between intact succinate:quinone oxidoreductase from Bacillus subtilis and a surface
modified gold electrode reveals redox state-dependent conformational changes. Biochim
Biophys Acta Bioenerg 1777:1203–1210.https://doi.org/10.1016/j.bbabio.2008.05.450
75. Barber MJ, Pollock V, Spence JT (1988) Microcoulometric analysis of trimethylamine
dehydrogenase. Biochem J 256:657–659. https://doi.org/10.1042/bj2560657
76. Husain M, Davidson VL, Gray KA, Knaff DB (1987) Redox properties of the quinoprotein
methylamine dehydrogenase from paracoccus denitrificans. Biochemistry 26:4139–4143.
https://doi.org/10.1021/bi00387a059
77. Kalimuthu P, Fischer-Schrader K, Schwarz G, Bernhardt PV (2013) Mediated Electrochemistry of Nitrate Reductase from Arabidopsis thaliana. J Phys Chem B 117:7569–7577.
https://doi.org/10.1021/jp404076w
78. Coelho C, Marangon J, Rodrigues D et al (2013) Induced peroxidase activity of haem
containing nitrate reductases revealed by protein film electrochemistry. J Electroanal Chem
693:105–113. https://doi.org/10.1016/j.jelechem.2013.01.030
79. Swamy U, Wang M, Tripathy JN et al (2005) Structure of Spinach Nitrite Reductase:
Implications for Multi-electron Reactions by the Iron − Sulfur: Siroheme Cofactor †, ‡.
Biochemistry 44:16054–16063. https://doi.org/10.1021/bi050981y
80. Cunha CA, Macieira S, Dias JM et al (2003) Cytochrome c nitrite reductase from
Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the
structure of the catalytic subunit (NrfA). J Biol Chem 278:17455–17465. https://doi.org/10.
1074/jbc.M211777200
81. Jacobson F, Pistorius A, Farkas D et al (2007) pH Dependence of Copper Geometry,
Reduction Potential, and Nitrite Affinity in Nitrite Reductase. J Biol Chem 282:6347–6355.
https://doi.org/10.1074/jbc.M605746200
82. Besson S, Carneiro C, Moura JJG et al (1995) A Cytochrome cd1-type Nitrite Reductase
Isolated from the Marine Denitrifier Pseudomonas nautica 617: Purification and Characterization. Anaerobe 1:219–226. https://doi.org/10.1006/anae.1995.1021
83. Gomes FO, Maia LB, Delerue-Matos C et al (2019) Third-generation electrochemical
biosensor based on nitric oxide reductase immobilized in a multiwalled carbon
nanotubes/1-n-butyl-3-methylimidazolium tetrafluoroborate nanocomposite for nitric oxide
detection. Sensors Actuators B Chem 285:445–452. https://doi.org/10.1016/j.snb.2019.01.
074
84. Bastian NR, Kay CJ, Barber MJ, Rajagopalan KV (1991) Spectroscopic studies of the
molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f.
sp. denitrificans. J Biol Chem 266:45–51
85. Mitrova B, Waffo AFT, Kaufmann P et al (2019) Trimethylamine N -Oxide Electrochemical
Biosensor with a Chimeric Enzyme. ChemElectroChem 6:1732–1737. https://doi.org/10.
1002/celc.201801422
86. Rakauskiene GA, Čenas NK, Kulys JJ (1989) A ‘branched’ mechanism of the reverse
reaction of yeast glutathione reductase An estimation of the enzyme standard potential
values from the steady-state kinetics data. FEBS Lett 243:33–36. https://doi.org/10.1016/
0014-5793(89)81212-8
87. Haynes CA, Koder RL, Miller A-F, Rodgers DW (2002) Structures of Nitroreductase in
Three States. J Biol Chem 277:11513–11520. https://doi.org/10.1074/jbc.M111334200
Selective Enzymes at the Core of Advanced Electroanalytical …
349
https://doi.org/10.1371/journal.pone.0115722
72. Larsson T, Lindgren A, Ruzgas T (2001) Spectroelectrochemical study of cellobiose
dehydrogenase and diaphorase in a thiol-modified gold capillary in the absence of mediators.
Bioelectrochemistry 53:243–249. https://doi.org/10.1016/S0302-4598(01)00099-X
73. Aguey-Zinsou KF, Bernhardt PV, Kappler U, McEwan AG (2003) Direct electrochemistry
of a bacterial sulfite dehydrogenase. J Am Chem Soc 125:530–535. https://doi.org/10.1021/
ja028293e
74. Christenson A, Gustavsson T, Gorton L, Hägerhäll C (2008) Direct and mediated electron
transfer between intact succinate:quinone oxidoreductase from Bacillus subtilis and a surface
modified gold electrode reveals redox state-dependent conformational changes. Biochim
Biophys Acta Bioenerg 1777:1203–1210.https://doi.org/10.1016/j.bbabio.2008.05.450
75. Barber MJ, Pollock V, Spence JT (1988) Microcoulometric analysis of trimethylamine
dehydrogenase. Biochem J 256:657–659. https://doi.org/10.1042/bj2560657
76. Husain M, Davidson VL, Gray KA, Knaff DB (1987) Redox properties of the quinoprotein
methylamine dehydrogenase from paracoccus denitrificans. Biochemistry 26:4139–4143.
https://doi.org/10.1021/bi00387a059
77. Kalimuthu P, Fischer-Schrader K, Schwarz G, Bernhardt PV (2013) Mediated Electrochemistry of Nitrate Reductase from Arabidopsis thaliana. J Phys Chem B 117:7569–7577.
https://doi.org/10.1021/jp404076w
78. Coelho C, Marangon J, Rodrigues D et al (2013) Induced peroxidase activity of haem
containing nitrate reductases revealed by protein film electrochemistry. J Electroanal Chem
693:105–113. https://doi.org/10.1016/j.jelechem.2013.01.030
79. Swamy U, Wang M, Tripathy JN et al (2005) Structure of Spinach Nitrite Reductase:
Implications for Multi-electron Reactions by the Iron − Sulfur: Siroheme Cofactor †, ‡.
Biochemistry 44:16054–16063. https://doi.org/10.1021/bi050981y
80. Cunha CA, Macieira S, Dias JM et al (2003) Cytochrome c nitrite reductase from
Desulfovibrio desulfuricans ATCC 27774. The relevance of the two calcium sites in the
structure of the catalytic subunit (NrfA). J Biol Chem 278:17455–17465. https://doi.org/10.
1074/jbc.M211777200
81. Jacobson F, Pistorius A, Farkas D et al (2007) pH Dependence of Copper Geometry,
Reduction Potential, and Nitrite Affinity in Nitrite Reductase. J Biol Chem 282:6347–6355.
https://doi.org/10.1074/jbc.M605746200
82. Besson S, Carneiro C, Moura JJG et al (1995) A Cytochrome cd1-type Nitrite Reductase
Isolated from the Marine Denitrifier Pseudomonas nautica 617: Purification and Characterization. Anaerobe 1:219–226. https://doi.org/10.1006/anae.1995.1021
83. Gomes FO, Maia LB, Delerue-Matos C et al (2019) Third-generation electrochemical
biosensor based on nitric oxide reductase immobilized in a multiwalled carbon
nanotubes/1-n-butyl-3-methylimidazolium tetrafluoroborate nanocomposite for nitric oxide
detection. Sensors Actuators B Chem 285:445–452. https://doi.org/10.1016/j.snb.2019.01.
074
84. Bastian NR, Kay CJ, Barber MJ, Rajagopalan KV (1991) Spectroscopic studies of the
molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f.
sp. denitrificans. J Biol Chem 266:45–51
85. Mitrova B, Waffo AFT, Kaufmann P et al (2019) Trimethylamine N -Oxide Electrochemical
Biosensor with a Chimeric Enzyme. ChemElectroChem 6:1732–1737. https://doi.org/10.
1002/celc.201801422
86. Rakauskiene GA, Čenas NK, Kulys JJ (1989) A ‘branched’ mechanism of the reverse
reaction of yeast glutathione reductase An estimation of the enzyme standard potential
values from the steady-state kinetics data. FEBS Lett 243:33–36. https://doi.org/10.1016/
0014-5793(89)81212-8
87. Haynes CA, Koder RL, Miller A-F, Rodgers DW (2002) Structures of Nitroreductase in
Three States. J Biol Chem 277:11513–11520. https://doi.org/10.1074/jbc.M111334200
Selective Enzymes at the Core of Advanced Electroanalytical …
349