Efficient Direct Electron Transfer of PQQ-glucose Dehydrogenase on Carbon Cryogel Electrodes at Neutral pH

2011 ◽  
Vol 83 (14) ◽  
pp. 5721-5727 ◽  
Author(s):  
Victoria Flexer ◽  
Fabien Durand ◽  
Seiya Tsujimura ◽  
Nicolas Mano
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase ◽  
Neutral Ph ◽  
Pqq Glucose Dehydrogenase ◽  
Carbon Cryogel

Designer fungus FAD glucose dehydrogenase capable of direct electron transfer

2019 ◽  
Vol 123 ◽  
pp. 114-123 ◽  
Author(s):  
Kohei Ito ◽  
Junko Okuda-Shimazaki ◽  
Kazushige Mori ◽  
Katsuhiro Kojima ◽  
Wakako Tsugawa ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase

In Vitro Evaluation of Miniaturized Amperometric Enzyme Sensor Based on the Direct Electron Transfer Principle for Continuous Glucose Monitoring

2022 ◽  
pp. 193229682110706
Author(s):  
Yutaro Inoue ◽  
Yasuhide Kusaka ◽  
Kotaro Shinozaki ◽  
Inyoung Lee ◽  
Koji Sode
Keyword(s):  
Electron Transfer ◽  
Continuous Glucose Monitoring ◽  
Glucose Sensor ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase ◽  
Glucose Monitoring ◽  
Reference Electrode ◽  
Enzyme Sensor

Background: The bacterial derived flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase (FADGDH) is the most promising enzyme for the third-generation principle-based enzyme sensor for continuous glucose monitoring (CGM). Due to the ability of the enzyme to transfer electrons directly to the electrode, recognized as direct electron transfer (DET)-type FADGDH, although no investigation has been reported about DET-type FADGDH employed on a miniaturized integrated electrode. Methods: The miniaturized integrated electrode was formed by sputtering gold (Au) onto a flexible film with 0.1 mm in thickness and divided into 3 parts. After an insulation layer was laminated, 3 openings for a working electrode, a counter electrode and a reference electrode were formed by dry etching. A reagent mix containing 1.2 × 10−4 Unit of DET-type FADGDH and carbon particles was deposited. The long-term stability of sensor was evaluated by continuous operation, and its performance was also evaluated in the presence of acetaminophen and the change in oxygen partial pressure (pO2) level. Results: The amperometric response of the sensor showed a linear response to glucose concentration up to 500 mg/dL without significant change of the response over an 11-day continuous measurement. Moreover, the effect of acetaminophen and pO2 on the response were negligible. Conclusions: These results indicate the superb potential of the DET-type FADGDH-based sensor with the combination of a miniaturized integrated electrode. Thus, the described miniaturized DET-type glucose sensor for CGM will be a promising tool for effective glycemic control. This will be further investigated using an in vivo study.

Third generation impedimetric sensor employing direct electron transfer type glucose dehydrogenase

2019 ◽  
Vol 129 ◽  
pp. 189-197 ◽  
Author(s):  
Yuka Ito ◽  
Junko Okuda-Shimazaki ◽  
Wakako Tsugawa ◽  
Noya Loew ◽  
Isao Shitanda ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase ◽  
Third Generation

scholarly journals X-ray structure of the direct electron transfer-type FAD glucose dehydrogenase catalytic subunit complexed with a hitchhiker protein

2019 ◽  
Vol 75 (9) ◽  
pp. 841-851 ◽  
Author(s):  
Hiromi Yoshida ◽  
Katsuhiro Kojima ◽  
Masaki Shiota ◽  
Keiichi Yoshimatsu ◽  
Tomohiko Yamazaki ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Disulfide Bonds ◽  
Hydrophobic Interactions ◽  
Direct Electron Transfer ◽  
Glucose Dehydrogenase ◽  
Catalytic Subunit ◽  
Effective Electron ◽  
Α Subunit ◽  
X Ray ◽  
Membrane Bound

The bacterial flavin adenine dinucleotide (FAD)-dependent glucose dehydrogenase complex derived from Burkholderia cepacia (BcGDH) is a representative molecule of direct electron transfer-type FAD-dependent dehydrogenase complexes. In this study, the X-ray structure of BcGDHγα, the catalytic subunit (α-subunit) of BcGDH complexed with a hitchhiker protein (γ-subunit), was determined. The most prominent feature of this enzyme is the presence of the 3Fe–4S cluster, which is located at the surface of the catalytic subunit and functions in intramolecular and intermolecular electron transfer from FAD to the electron-transfer subunit. The structure of the complex revealed that these two molecules are connected through disulfide bonds and hydrophobic interactions, and that the formation of disulfide bonds is required to stabilize the catalytic subunit. The structure of the complex revealed the putative position of the electron-transfer subunit. A comparison of the structures of BcGDHγα and membrane-bound fumarate reductases suggested that the whole BcGDH complex, which also includes the membrane-bound β-subunit containing three heme c moieties, may form a similar overall structure to fumarate reductases, thus accomplishing effective electron transfer.

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