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252. Yu J, Zhou C-Z (2007) Crystal structure of glutathione reductase Glr1 from the yeast
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1002/prot.21354
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114:10965–10966. https://doi.org/10.1021/ja00053a045
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255. Corrêa CC, Santhiago M, Formiga ALB, Kubota LT (2013) In situ activated nanostructured
platform for oxidized glutathione biosensing. Electrochim Acta 90:309–316. https://doi.org/
10.1016/j.electacta.2012.12.046
256. Crofts AR (2004) The Cytochrome bc 1 Complex: Function in the Context of Structure.
Annu Rev Physiol 66:689–733. https://doi.org/10.1146/annurev.physiol.66.032102.150251
257. Santharaman P, Venkatesh KA, Vairamani K et al (2017) ARM-microcontroller based
portable nitrite electrochemical analyzer using cytochrome c reductase biofunctionalized
onto screen printed carbon electrode. Biosens Bioelectron 90:410–417. https://doi.org/10.
1016/j.bios.2016.10.039
258. Navaee A, Salimi A (2019) Enzyme-based electrochemical biosensors. In: Electrochemical
Biosensors. Elsevier, pp 167–211
259. Colovic MB, Krstic DZ, Lazarevic-Pasti TD et al (2013) Acetylcholinesterase Inhibitors:
Pharmacology and Toxicology. Curr Neuropharmacol 11:315–335. https://doi.org/10.2174/
1570159X11311030006
260. Latip W, Knight VF, Abdul Halim N et al (2019) Microbial Phosphotriesterase: Structure,
Function, and Biotechnological Applications. Catalysts 9:671. https://doi.org/10.3390/
catal9080671
261. Trojanowicz M (2002) Determination of Pesticides Using Electrochemical Enzymatic
Biosensors. Electroanalysis 14:1311–1328. https://doi.org/10.1002/1521-4109(200211)14:
19/20%3c1311:AID-ELAN1311%3e3.0.CO;2-7
262. Pundir CS, Malik A, Preety (2019) Bio-sensing of organophosphorus pesticides: a review.
Biosens Bioelectron 140:111348. https://doi.org/10.1016/j.bios.2019.111348
263. Schöning MJ, Krause R, Block K et al (2003) A dual amperometric/potentiometric
FIA-based biosensor for the distinctive detection of organophosphorus pesticides. Sensors
Actuators B Chem 95:291–296. https://doi.org/10.1016/S0925-4005(03)00426-X
Selective Enzymes at the Core of Advanced Electroanalytical …
359
127:76–86. https://doi.org/10.1016/j.bioelechem.2019.01.010
247. Kaufmann P, Duffus BR, Mitrova B et al (2018) Modulating the Molybdenum Coordination
Sphere of Escherichia coli Trimethylamine N -Oxide Reductase. Biochemistry 57:1130–
1143. https://doi.org/10.1021/acs.biochem.7b01108
248. Schindelin H, Kisker C, Hilton J, et al (1996) Crystal Structure of DMSO Reductase:
Redox-Linked Changes in Molybdopterin Coordination. Science (80-) 272:1615–1621.
https://doi.org/10.1126/science.272.5268.1615
249. Youngblut MD, Tsai C-L, Clark IC et al (2016) Perchlorate Reductase Is Distinguished by
Active Site Aromatic Gate Residues. J Biol Chem 291:9190–9202. https://doi.org/10.1074/
jbc.M116.714618
250. Yonehara H, Fujii S, Sato K et al (2007) Construction of a Dimethyl Sulfoxide Sensor Based
on Dimethyl Sulfoxide Reductase Immobilized on a Au Film Electrode. Anal Sci 23:55–58.
https://doi.org/10.2116/analsci.23.55
251. Timur S, Odaci D, Dincer A et al (2008) Biosensing approach for glutathione detection using
glutathione reductase and sulfhydryl oxidase bienzymatic system. Talanta 74:1492–1497.
https://doi.org/10.1016/j.talanta.2007.09.026
252. Yu J, Zhou C-Z (2007) Crystal structure of glutathione reductase Glr1 from the yeast
Saccharomyces cerevisiae. Proteins Struct Funct Bioinforma 68:972–979. https://doi.org/10.
1002/prot.21354
253. Willner I, Katz E, Riklin A, Kasher R (1992) Mediated electron transfer in gluthathione
reductase organized in self-assembled monolayers on gold electrodes. J Am Chem Soc
114:10965–10966. https://doi.org/10.1021/ja00053a045
254. Carano M, Cosnier S, Kordatos K et al (2002) A glutathione amperometric biosensor based
on an amphiphilic fullerene redox mediator immobilised within an amphiphilic polypyrrole
film. J Mater Chem 12:1996–2000. https://doi.org/10.1039/b201469f
255. Corrêa CC, Santhiago M, Formiga ALB, Kubota LT (2013) In situ activated nanostructured
platform for oxidized glutathione biosensing. Electrochim Acta 90:309–316. https://doi.org/
10.1016/j.electacta.2012.12.046
256. Crofts AR (2004) The Cytochrome bc 1 Complex: Function in the Context of Structure.
Annu Rev Physiol 66:689–733. https://doi.org/10.1146/annurev.physiol.66.032102.150251
257. Santharaman P, Venkatesh KA, Vairamani K et al (2017) ARM-microcontroller based
portable nitrite electrochemical analyzer using cytochrome c reductase biofunctionalized
onto screen printed carbon electrode. Biosens Bioelectron 90:410–417. https://doi.org/10.
1016/j.bios.2016.10.039
258. Navaee A, Salimi A (2019) Enzyme-based electrochemical biosensors. In: Electrochemical
Biosensors. Elsevier, pp 167–211
259. Colovic MB, Krstic DZ, Lazarevic-Pasti TD et al (2013) Acetylcholinesterase Inhibitors:
Pharmacology and Toxicology. Curr Neuropharmacol 11:315–335. https://doi.org/10.2174/
1570159X11311030006
260. Latip W, Knight VF, Abdul Halim N et al (2019) Microbial Phosphotriesterase: Structure,
Function, and Biotechnological Applications. Catalysts 9:671. https://doi.org/10.3390/
catal9080671
261. Trojanowicz M (2002) Determination of Pesticides Using Electrochemical Enzymatic
Biosensors. Electroanalysis 14:1311–1328. https://doi.org/10.1002/1521-4109(200211)14:
19/20%3c1311:AID-ELAN1311%3e3.0.CO;2-7
262. Pundir CS, Malik A, Preety (2019) Bio-sensing of organophosphorus pesticides: a review.
Biosens Bioelectron 140:111348. https://doi.org/10.1016/j.bios.2019.111348
263. Schöning MJ, Krause R, Block K et al (2003) A dual amperometric/potentiometric
FIA-based biosensor for the distinctive detection of organophosphorus pesticides. Sensors
Actuators B Chem 95:291–296. https://doi.org/10.1016/S0925-4005(03)00426-X
Selective Enzymes at the Core of Advanced Electroanalytical …
359