Direct Bioelectrocatalysis at Metal and Carbon Electrodes Modified with Adsorbed <scp>d</scp>-Gluconate Dehydrogenase or Adsorbed Alcohol Dehydrogenase from Bacterial Membranes

Ikeda, Tokuji; Miyaoka, Shuji; Matsushita, Fumio; Kobayashi, Daisuke; Senda, Mitsugi

doi:10.1246/cl.1992.847

Cited by 26 publications

(8 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Indeed, many redox proteins involved in photosynthesis and metabolism are located in the mitochondrial, chloroplast or plasma [7] membranes. However, because membrane proteins are more difficult to manipulate experimentally than globular proteins, less work has been reported on the electrochemistry of these proteins[8, 9, 10, 11, 12, 13, 14, 15, 16, 17]. One of the foregoing successful strategies is to reconstitute purified and detergent-solubilised proteins in a biomimicking membrane on the surface[12, 13, 14, 15, 16, 17].…”

Section: Introductionmentioning

confidence: 99%

Direct Electrochemical Interaction between a Modified Gold Electrode and a Bacterial Membrane Extract

et al. 2005

View full text Add to dashboard Cite

A novel electrochemical approach is described for redox-active membrane proteins. A total membrane extract (in the form of vesicles) of Bacillus subtilis is tethered onto gold surfaces modified with cholesterol based thiols. The membrane vesicles remain intact on the surface and do not rupture or fuse to form a planar bilayer. Oxidation/reduction signals are obtained of the natural co-enzyme, menaquinone-7, located in the membrane. The membrane protein, succinate menaquinone oxidoreductase (SQR), remains in the vesicles and is able to reduce fumarate using menaquinone as mediator. The catalysis of the reverse reaction (oxidation of succinate), which is the natural catalytic function of SQR, is almost absent with menaquinone. However, adding the co-enzyme ubiquinone, which has a reduction potential that is about 0.2 V higher, restores the succinate oxidation activity.

show abstract

Section: Introductionmentioning

confidence: 99%

Direct Electrochemical Interaction between a Modified Gold Electrode and a Bacterial Membrane Extract

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Recently, multicofactor enzymes, mostly consisting of more than one subunit, such as pyrroloquinoline-quinone (PQQ) and heme-containing enzymes ( d -fructose dehydrogenase, , alcohol dehydrogenase) or FAD and heme containing enzymes ( p -cresolmethylhydroxylase, fumarate reductase, flavocytochrome c 552 , d -gluconate dehydrogenase, and cellobiose dehydrogenase), were shown to display a direct ET mechanism , when immobilized on various electrode materials. The proposed mechanism assumes that the ET pathway between the enzyme's active center and an electrode consists of distinct ET steps between the individual electron-exchange sites, confirming the importance of the distance separating the active site from the electrode, well in agreement with Marcus theory. , Thus, a multiredox-center enzyme can be seen as a combination of a primary redox site and protein-integrated electron-transfer relays.…”

mentioning

confidence: 99%

Polypyrrole-Entrapped Quinohemoprotein Alcohol Dehydrogenase. Evidence for Direct Electron Transfer via Conducting-Polymer Chains

et al. 1999

View full text Add to dashboard Cite

It is reported for the first time that direct electron-transfer processes between a polypyrrole (PPY) entrapped quinohemoprotein alcohol dehydrogenase from Gluconobacter sp. 33 (QH-ADH) and a platinum electrode take place via the conducting-polymer network. The cooperative action of the enzyme-integrated prosthetic groups--pyrroloquinoline-quinone and hemes--is assumed to allow this electron-transfer pathway from the enzyme's active site to the conducting-polymer backbone. A hypothetical model of the electron transfer is proposed which is supported by the influence of various parameters, such as, e.g., ionic strength and nature of the buffer salts. This unusual electron-transfer pathway leads to an accentuated increase of the K M app value (102 mM) and hence to a significantly increased linear detection range of an ethanol sensor based on this enzyme.

show abstract

“…Despite the prevalence of electrode modification types of the above-named categories in the design of amperometric DET-based biosensors, several exceptions, that is, biosensors getting along without any electrode modification, have to be recognized. The first example is D-gluconate dehydrogenase, and it was reported to perform DET on bare glassy carbon, carbon paste, indium tin oxide (ITO) and gold electrodes without creating any mesoporous structure or modifying any nanomaterials or SAMs [ 121 , 122 , 123 ]. In these studies, the enzyme was generally adsorbed on the bare electrodes and was able to produce a pair of well-defined current peaks.…”

Section: Electrode Materials and Modificationsmentioning

confidence: 99%

Amperometric Biosensors Based on Direct Electron Transfer Enzymes

et al. 2021

View full text Add to dashboard Cite

The accurate determination of analyte concentrations with selective, fast, and robust methods is the key for process control, product analysis, environmental compliance, and medical applications. Enzyme-based biosensors meet these requirements to a high degree and can be operated with simple, cost efficient, and easy to use devices. This review focuses on enzymes capable of direct electron transfer (DET) to electrodes and also the electrode materials which can enable or enhance the DET type bioelectrocatalysis. It presents amperometric biosensors for the quantification of important medical, technical, and environmental analytes and it carves out the requirements for enzymes and electrode materials in DET-based third generation biosensors. This review critically surveys enzymes and biosensors for which DET has been reported. Single- or multi-cofactor enzymes featuring copper centers, hemes, FAD, FMN, or PQQ as prosthetic groups as well as fusion enzymes are presented. Nanomaterials, nanostructured electrodes, chemical surface modifications, and protein immobilization strategies are reviewed for their ability to support direct electrochemistry of enzymes. The combination of both biosensor elements—enzymes and electrodes—is evaluated by comparison of substrate specificity, current density, sensitivity, and the range of detection.

show abstract

Direct Bioelectrocatalysis at Metal and Carbon Electrodes Modified with Adsorbed d-Gluconate Dehydrogenase or Adsorbed Alcohol Dehydrogenase from Bacterial Membranes

Cited by 26 publications

References 10 publications

Direct Electrochemical Interaction between a Modified Gold Electrode and a Bacterial Membrane Extract

Direct Electrochemical Interaction between a Modified Gold Electrode and a Bacterial Membrane Extract

Polypyrrole-Entrapped Quinohemoprotein Alcohol Dehydrogenase. Evidence for Direct Electron Transfer via Conducting-Polymer Chains

Amperometric Biosensors Based on Direct Electron Transfer Enzymes

Contact Info

Product

Resources

About