The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme

Hecht, Hans‐Jürgen; Schomburg, Dietmar; Kalisz, Henryk M.; Schmid, Rolf D.

doi:10.1016/0956-5663(93)85033-k

Cited by 157 publications

(111 citation statements)

References 6 publications

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“…5,6,[9][10][11] FOD AO was crystallized in space group C222 1 (Table 1), in which three subunits are contained in the asymmetric unit. FOD AO has been found to be a dimeric protein in solution by size-exclusion chromatography and SDS-PAGE.…”

Section: Discussionmentioning

confidence: 99%

“…Although they exhibit low amino acid sequence similarities at their catalytic sites, 1) the crystal structures of the enzymes, such as cholesterol oxidase, [2][3][4] glucose oxidase, 5,6) pyranose 2-oxidase, 7,8) choline oxidase, [9][10][11] and arylalcohol oxidase, 12) show that all of them share a highly conserved catalytic site. In the vicinity of the pyrimidine part of the isoalloxazine ring, a His residue conserved through this family of enzymes pairs with an Asn residue or a His residue.…”

mentioning

confidence: 99%

“…[20][21][22] In the choline and glucose oxidases, the His 466 -Asn 510 and His 516 -His 559 pairs respectively are situated close to the pyrimidine part of the isoalloxazine ring, respectively. 5,6,9) Comparisons of the amino acid sequences of the FODs with those of the choline and glucose oxidases suggest that the His 511 -Arg 554 pair and the His 508 -Arg 551 pair are situated close to the pyrimidine part of the isoalloxazine ring in recombinant Aspergillus oryzae FOD (FOD AO ) and the Debaryomyces FODs respectively.…”

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confidence: 99%

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Formate Oxidase, an Enzyme of the Glucose-Methanol-Choline Oxidoreductase Family, Has a His-Arg Pair and 8-Formyl-FAD at the Catalytic Site

Doubayashi¹,

Ootake²,

Maeda³

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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Formate Oxidase, an Enzyme of the Glucose-Methanol-Choline Oxidoreductase Family, Has a His-Arg Pair and 8-Formyl-FAD at the Catalytic Site

Doubayashi¹,

Ootake²,

Maeda³

et al. 2011

Bioscience, Biotechnology, and Biochemistry

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“…The latter process has the advantages that it avoids possible leakage and diffusional limitations associated with the use of mediators. However, the redox active centers of GOx are deeply buried with a minimal distance of 13-18 Å between the periphery of GOx and the N7 nitrogen of the isoalloxazine rings of FAD [65]. Achieving DET of GOx (third-generation glucose biosensors [63]) has been hampered by requirements including optimization of enzyme 40 orientation and minimization of the distance between the active center of the enzyme and the surface of the electrode .…”

Section: Enzyme Based Glucose Biosensorsmentioning

confidence: 99%

An overview of dealloyed nanoporous gold in bioelectrochemistry

Xiao

Magner

2016

Bioelectrochemistry

104

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“…This loading however, does not correspond to close packing of the enzyme on the SAM surface. Based on the size of glucose oxidase molecule of 7 × 5.5 × 8 nm, 51 the theoretical maximum enzyme loading is 2.6 -3.8 pmol cm -2 . The lower density of enzyme packing on the surface is confirmed by tapping mode AFM images of these enzyme-modified surfaces.…”

Section: Immobilization Conditionsmentioning

confidence: 99%

Parameters Important in Fabricating Enzyme Electrodes Using Self-Assembled Monolayers of Alkanethiols

et al. 2001

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The immobilization of enzymes on the surface of electrodes modified with self-assembled monolayers (SAMs) provides a number of advantages as a method for the fabrication of enzyme electrodes. Using SAMs has the potential to provide enzyme electrodes with a high degree of reproducibility, 1,2 molecular level control over the spatial distribution of the immobilized enzymes 3-14 and the immobilization of the enzyme close to the electrode thus allowing direct electron transfer to be achieved. [15][16][17][18][19][20][21][22][23][24] These advantages have resulted in a recent surge in research into self-assembled monolayers for biosensor applications in general, and enzyme electrodes in particular. [25][26][27] However, despite the plethora of biosensor research papers using self-assembled monolayers as the base onto which the biomolecule is immobilized, there has been very little fundamental research into what steps are important in the fabrication process or which parameters control the response of the resultant biosensor.Alkanethiols modifying gold are the most popular SAMs. 25,26 The interaction between the thiol groups and the gold results in a strong pseudocovalent bond 28 which is stable throughout the potential range of 0.8 V to -1.4 V versus Ag/AgCl before being oxidatively or reductively desorbed. 29,30 If the alkanethiol has appropriate chemical functionality, such as an amine or carboxylic acid moiety, then once the SAM is formed, enzymes and other biomolecules can be easily covalently bound to the SAM. In this way, a monolayer or submonolayer of enzyme is immobilized. For enzyme electrodes a short alkyl chain alkanethiol, usually three carbons long, is chosen so that the enzyme is as close as possible to the electrode. An additional advantage of the short alkyl chain is that a relatively disordered SAM is formed which means the underlying metal is still electrochemically accessible. In contrast, if a long chain alkanethiol is used the electrode is passivated unless defects are deliberately introduced into the SAM. 31 There are a number of steps in the fabrication of an enzyme electrode using an alkanethiol. First, the metal surface must be prepared and cleaned. The alkanethiol must self-assemble onto the metal, followed by activation of the chemical functionality of the SAM, leading finally to the exposure of the activated SAM to the enzyme which is when attachment occurs. There are however many unknowns in this fabrication process. Questions that needs answers are: what effect does the roughness of the gold surface have? How long should the metal be exposed to the alkanethiol solution to allow a stable SAM to be formed? What is the optimal procedure for activating the SAM for enzyme attachment? How long should the activated SAM be exposed to enzyme? What should the concentration of the enzyme solution be during enzyme immobilization? Does the buffer used have any effect on subsequent performance? Can the amount of enzyme immobilized be controlled and do different enzyme loadings lead to different electr...

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The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme

Cited by 157 publications

References 6 publications

Formate Oxidase, an Enzyme of the Glucose-Methanol-Choline Oxidoreductase Family, Has a His-Arg Pair and 8-Formyl-FAD at the Catalytic Site

Formate Oxidase, an Enzyme of the Glucose-Methanol-Choline Oxidoreductase Family, Has a His-Arg Pair and 8-Formyl-FAD at the Catalytic Site

An overview of dealloyed nanoporous gold in bioelectrochemistry

Parameters Important in Fabricating Enzyme Electrodes Using Self-Assembled Monolayers of Alkanethiols

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