269 - Polarographic reduction of the prosthetic group in flavoproteins

Early Polarographic Studies on Proteins

“…From polarographic behavior of cytochrome c 3 it was concluded that the 4 hemes per molecule accept stepwise 4 electrons in course of reduction [57]. In polarographic study of bacteriorhodopsin a one-electron reduction of retinal was identified [58], in flavoproteins it was proved by polarography that the prosthetic group is riboflavin [59]. Differential pulse polarography has done its service in research on metallothioneins [60], polarography helped in the study of zinc binding to glutamate dehydrogenase [61].…”

Direct electron transfer of glucose oxidase immobilized in an ionic liquid reconstituted cellulose–carbon nanotube matrix

“…2B). The peaks are attributable to the reduction and oxidation of the FAD/FADH 2 electroactive centre of the GOx enzyme by a direct electron transfer process (reaction 1) [25]; redox peaks were not observed with a protein-free cellulose-MWCNT modified electrode in the potential range -650 to 0 mV.…”

A Homogenous Assay of FAD Using a Binding Between Apo‐Glucose Oxidase and FAD Labeled with an Electroactive Compound

“…The peak current of 5.0 Â 10 À7 M FAD without the accumulation was similar to that after accumulation for 5 min. It is known that FAD strongly adsorbs to a mercury electrode [11]. In contrast, this result shows that the adsorption ability of FAD to the glassy carbon electrode is low.…”

“…Since FAD is an electroactivity, the behavior of FAD in a solution was investigated with an electrochemical procedure. Scheller et al has reported reduction at D. M. E of the prosthetic group in GOD and riboflavin flavoprotein [11]. The detection of FAD is carried out with an electrochemical chromatography [12].…”