2018
DOI: 10.1016/j.elecom.2018.06.010
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Magnetic-field-induced orientation of fructose dehydrogenase on iron oxide nanoparticles for enhanced direct electron transfer

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Cited by 12 publications
(11 citation statements)
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“…Recently, the magnetic‐field‐induced orientation of fructose dehydrogenase on iron oxide nanoparticles for enhanced direct electron transfer (DET) has been reported . In this study, the magnetic interactions between the paramagnetic heme groups of fructose dehydrogenase subunit II and superparamagnetic iron oxide nanoparticles enables a suitable orientation of the enzyme molecule and enhance the rate of DET …”
Section: Introductionmentioning
confidence: 95%
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“…Recently, the magnetic‐field‐induced orientation of fructose dehydrogenase on iron oxide nanoparticles for enhanced direct electron transfer (DET) has been reported . In this study, the magnetic interactions between the paramagnetic heme groups of fructose dehydrogenase subunit II and superparamagnetic iron oxide nanoparticles enables a suitable orientation of the enzyme molecule and enhance the rate of DET …”
Section: Introductionmentioning
confidence: 95%
“…Electrochemical reactions, including bioelectrocatalytic and electrocatalytic processes, have been reversibly activated and inhibited upon physical translocation and reorientation of different magnetic micro/nano‐species on the electrode surface, particularly using magnetic micro‐and nanoparticles . Recently, the magnetic‐field‐induced orientation of fructose dehydrogenase on iron oxide nanoparticles for enhanced direct electron transfer (DET) has been reported . In this study, the magnetic interactions between the paramagnetic heme groups of fructose dehydrogenase subunit II and superparamagnetic iron oxide nanoparticles enables a suitable orientation of the enzyme molecule and enhance the rate of DET …”
Section: Introductionmentioning
confidence: 97%
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“…Many papers present effective bioelectrocatalytical processes, where several mono- and multi-cofactor redox enzymes [7], such as cellobiose dehydrogenase [5, 8, 9], horseradish peroxidase, superoxide dismutase, fructose dehydrogenase [1012], blue multicopper oxidases (MCOs) [13, 14], and human sulfite oxidase [15], have been immobilized onto nanostructured electrodes. Despite the large interest in AuNPs, there are only few reports about the influence of the size (e.g., diameter) and shape of the NPs on the enzymatic reactions occurring at the electrodes, sometimes improving the ET rate or changing the mechanism of the bioelectrocatalytic process [16, 17].…”
Section: Introductionmentioning
confidence: 99%