| |
Records |
Links |
|
Author |
Lybaert, J.; Trashin, S.; Maes, B.U.W.; De Wael, K.; Abbaspour Tehrani, K. |
|
| |
Title |
Cooperative electrocatalytic and chemoselective alcohol oxidation by Shvo's catalyst |
Type |
A1 Journal article |
| |
Year |
2017 |
Publication |
Advanced synthesis and catalysis |
Abbreviated Journal |
Adv Synth Catal |
|
| |
Volume |
359 |
Issue |
6 |
Pages |
919-925 |
|
| |
Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation); Organic synthesis (ORSY) |
|
| |
Abstract |
A new electrocatalytic conversion of alcohols to ketones and aldehydes was developed based on an electrochemical study of Shvos complex. The oxidation of secondary alcohols was efficiently performed under mild conditions using a catalytic amount of Shvos catalyst, in combination with a sub-stoichiometric amount of 2,6-dimethoxy-1,4- benzoquinone in N,N-dimethylformamide at 80 8C. The hydroquinone thus formed is continuously reoxidized with the aid of an electrochemical device. Excellent yields for different ketones, aromatic as well as aliphatic and a,b-unsaturated ketones, are obtained. In addition, chemoselectivity towards oxidation of the secondary alcohol is achieved when converting vicinal diols such as 1,2-octanediol and 1,2-decanediol. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Wos |
000397584000003 |
Publication Date |
2017-01-26 |
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
1615-4150; 1615-4169 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
|
| |
Impact Factor |
5.646 |
Times cited |
4 |
Open Access |
|
|
| |
Notes |
; This work was financially supported by the University of Antwerp (BOF), the Research Foundation – Flanders (FWO) and the Hercules Foundation. ; |
Approved |
Most recent IF: 5.646 |
|
| |
Call Number |
UA @ admin @ c:irua:139795 |
Serial  |
5559 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Trashin, S.; De Jong, M.; Meynen, V.; Dewilde, S.; De Wael, K. |
|
| |
Title |
Attaching redox proteins onto electrode surfaces by bis-silane |
Type |
A1 Journal article |
| |
Year |
2016 |
Publication |
ChemElectroChem |
Abbreviated Journal |
Chemelectrochem |
|
| |
Volume |
3 |
Issue |
7 |
Pages |
1035-1038 |
|
| |
Keywords |
A1 Journal article; Laboratory of adsorption and catalysis (LADCA); AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
|
| |
Abstract |
Immobilization of redox proteins on electrode surfaces is of special interest for mechanistic studies and applications because of a well-controlled redox state of protein molecules by a polarized electrode and fast electron transfer kinetics, free from diffusion limitation. Here, bis-organosilane (1,2-bis(trimethoxysilyl)ethane) was applied as a fresh solution in a pH 7 phosphate buffer without use of any organic solvent, sol-gel or mesoporous bulk matrix. A short aging period of 30 minutes before deposition on the electrodes was optimal for the immobilization of proteins. Three redox proteins (cytochrome c, neuroglobin and GLB-12) were confined to the gold surface of electrodes with high coverages and stability, indicating that the suggested technique is simple, efficient and generic in nature. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Wos |
000380043500001 |
Publication Date |
2016-03-09 |
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
2196-0216 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
|
| |
Impact Factor |
4.136 |
Times cited |
4 |
Open Access |
|
|
| |
Notes |
; The authors thank the Fund for Scientific Research-Flanders (FWO) (Grant G.0687.13) and the GOA-BOF UA 2013-2016 (project ID 28312) for funding. ; |
Approved |
Most recent IF: 4.136 |
|
| |
Call Number |
UA @ admin @ c:irua:132628 |
Serial |
5485 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Cuypers, B.; Vermeylen, S.; Hammerschmid, D.; Trashin, S.; Rahemi, V.; Konijnenberg, A.; De Schutter, A.; Cheng, C.-H.C.; Giordano, D.; Verde, C.; De Wael, K.; Sobott, F.; Dewilde, S.; Van Doorslaer, S. |
|
| |
Title |
Antarctic fish versus human cytoglobins : the same but yet so different |
Type |
A1 Journal article |
| |
Year |
2017 |
Publication |
Journal of inorganic biochemistry |
Abbreviated Journal |
J Inorg Biochem |
|
| |
Volume |
173 |
Issue |
|
Pages |
66-78 |
|
| |
Keywords |
A1 Journal article; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
|
| |
Abstract |
The cytoglobins of the Antarctic fish Chaenocephalus aceratus and Dissostichus mawsoni have many features in common with human cytoglobin. These cytoglobins are heme proteins in which the ferric and ferrous forms have a characteristic hexacoordination of the heme iron, i.e. axial ligation of two endogenous histidine residues, as confirmed by electron paramagnetic resonance, resonance Raman and optical absorption spectroscopy. The combined spectroscopic analysis revealed only small variations in the heme-pocket structure, in line with the small variations observed for the redox potential. Nevertheless, some striking differences were also discovered. Resonance Raman spectroscopy showed that the stabilization of an exogenous heme ligand, such as CO, occurs differently in human cytoglobin in comparison with Antarctic fish cytoglobins. Furthermore, while it has been extensively reported that human cytoglobin is essentially monomeric and can form an intramolecular disulfide bridge that can influence the ligand binding kinetics, 3D modeling of the Antarctic fish cytoglobins indicates that the cysteine residues are too far apart to form such an intramolecular bridge. Moreover, gel filtration and mass spectrometry reveal the occurrence of non-covalent multimers (up to pentamers) in the Antarctic fish cytoglobins that are formed at low concentrations. Stabilization of these oligomers by disulfide-bridge formation is possible, but not essential. If intermolecular disulfide bridges are formed, they influence the heme-pocket structure, as is shown by EPR measurements. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Wos |
000405159600007 |
Publication Date |
2017-04-28 |
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0162-0134 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
|
| |
Impact Factor |
3.348 |
Times cited |
7 |
Open Access |
|
|
| |
Notes |
; The authors acknowledge the support of the University of Antwerp GOA-BOF funding (28312), FWO funding (G.0687.13) and the Hercules foundation for funding of the Synapt G2 instrument. This study was carried out in the framework of the SCAR program “Antarctic Thresholds – Ecosystem Resilience and Adaptation” (AnT-ERA). It was financially supported by the Italian National Program for Antarctic Research (PNRA). Research of A. De Schutter is funded by a PhD grant of the Agency for Innovation by Science and Technology (121339) (IWT, Belgium). C-H C. Cheng acknowledges funding support from US National Science Foundation Polar Programs (ANT-1142158). ; |
Approved |
Most recent IF: 3.348 |
|
| |
Call Number |
UA @ admin @ c:irua:144826 |
Serial |
5474 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Rahemi, V.; Trashin, S.; Hafideddine, Z.; Van Doorslaer, S.; Meynen, V.; Gorton, L.; De Wael, K. |
|
| |
Title |
Amperometric flow-injection analysis of phenols induced by reactive oxygen species generated under daylight irradiation of titania impregnated with horseradish peroxidase |
Type |
A1 Journal article |
| |
Year |
2020 |
Publication |
Analytical Chemistry |
Abbreviated Journal |
Anal Chem |
|
| |
Volume |
92 |
Issue |
92 |
Pages |
3643-3649 |
|
| |
Keywords |
A1 Journal article; Laboratory of adsorption and catalysis (LADCA); AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
|
| |
Abstract |
Titanium dioxide (TiO2) is a unique material for biosensing applications due to its capability of hosting enzymes. For the first time, we show that TiO2 can accumulate reactive oxygen species (ROS) under daylight irradiation and can support the catalytic cycle of horseradish peroxidase (HRP) without the need of H2O2 to be present in the solution. Phenolic compounds, such as hydroquinone (HQ) and 4-aminophenol (4-AP), were detected amperometrically in flow-injection analysis (FIA) mode via the use of an electrode modified with TiO2 impregnated with HRP. In contrast to the conventional detection scheme, no H2O2 was added to the analyte solution. Basically, the inherited ability of TiO2 to generate reactive oxygen species is used as a strategy to avoid adding H2O2 in the solution during the detection of phenolic compounds. Electron paramagnetic resonance (EPR) spectroscopy indicates the presence of ROS on titania which, in interaction with HRP, initiate the electrocatalysis toward phenolic compounds. The amperometric response to 4-AP was linear in the concentration range between 0.05 and 2 μM. The sensitivity was 0.51 A M–1 cm–2, and the limit of detection (LOD) 26 nM. The proposed sensor design opens new opportunities for the detection of phenolic traces by HRP-based electrochemical biosensors, yet in a more straightforward and sensitive way following green chemistry principles of avoiding the use of reactive and harmful chemical, such as H2O2. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Wos |
000518234700023 |
Publication Date |
2020-01-27 |
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0003-2700; 5206-882x |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
|
| |
Impact Factor |
7.4 |
Times cited |
3 |
Open Access |
|
|
| |
Notes |
; The authors thank Scientific Reseatch-Flanders (F-WO) (grant 12T4219N) for funding. ; |
Approved |
Most recent IF: 7.4; 2020 IF: 6.32 |
|
| |
Call Number |
UA @ admin @ c:irua:166241 |
Serial |
5463 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Rahemi, V.; Trashin, S.; Meynen, V.; De Wael, K. |
|
| |
Title |
An adhesive conducting electrode material based on commercial mesoporous titanium dioxide as a support for Horseradish peroxidase for bioelectrochemical applications |
Type |
A1 Journal article |
| |
Year |
2016 |
Publication |
Talanta : the international journal of pure and applied analytical chemistry |
Abbreviated Journal |
Talanta |
|
| |
Volume |
146 |
Issue |
|
Pages |
689-693 |
|
| |
Keywords |
A1 Journal article; Laboratory of adsorption and catalysis (LADCA); AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
|
| |
Abstract |
An adhesive conducting electrode material containing of graphite, biocompatible ion exchange polymer nafion® and commercial mesoporous TiO2 impregnated with horseradish peroxidase (HRP) is prepared and characterized by amperometric, UVvis and N2 sorption methods. The factors influencing the performance of the resulting biosensor are studied in detail. The optimal electrode material consists of 45% graphite, 50% impregnated HRPTiO2 and 5% nafion®. The optimum conditions for H2O2 reduction are an applied potential of 0.3 V and 0.1 mM hydroquinone. Sensitivity and limit of detection in the optimum conditions are 1 A M−1 cm−2 and 1 µM correspondingly. The N2 sorption results show that the pore volume of TiO2 decreases sharply upon adsorption of HRP. The preparation process of the proposed enzyme electrode is straightforward and potentially can be used for preparation of carbon paste electrodes for bioelectrochemical detections. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Wos |
000363815600093 |
Publication Date |
2015-06-24 |
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
0039-9140; 1873-3573 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
|
| |
Impact Factor |
4.162 |
Times cited |
7 |
Open Access |
|
|
| |
Notes |
; The authors thank the Fund for Scientific Research – Flanders (FWO) (Grant G.0687.13), the GOA-BOF UA 2013-2016 (project-ID 28312) for funding and Ward Huybrechts of the University of Antwerp, Laboratory of Adsorption and Catalysis (LADCA) for help with the N<INF>2</INF> sorption. ; |
Approved |
Most recent IF: 4.162 |
|
| |
Call Number |
UA @ admin @ c:irua:126495 |
Serial |
5458 |
|
| Permanent link to this record |
| |
|
| |
|
Author |
Meysman, F.J.R.; Cornelissen, R.; Trashin, S.; Bonne, R.; Hidalgo-Martinez, S.; van der Veen, J.; Blom, C.J.; Karman, C.; Hou, J.-L.; Eachambadi, R.T.; Geelhoed, J.S.; De Wael, K.; Beaumont, H.J.E.; Cleuren, B.; Valcke, R.; van der Zant, H.S.J.; Boschker, H.T.S.; Manca, J.V. |
|
| |
Title |
A highly conductive fibre network enables centimetre-scale electron transport in multicellular cable bacteria |
Type |
A1 Journal article |
| |
Year |
2019 |
Publication |
Nature communications |
Abbreviated Journal |
Nat Commun |
|
| |
Volume |
10 |
Issue |
10 |
Pages |
4120 |
|
| |
Keywords |
A1 Journal article; Engineering sciences. Technology; AXES (Antwerp X-ray Analysis, Electrochemistry and Speciation) |
|
| |
Abstract |
Biological electron transport is classically thought to occur over nanometre distances, yet recent studies suggest that electrical currents can run along centimetre-long cable bacteria. The phenomenon remains elusive, however, as currents have not been directly measured, nor have the conductive structures been identified. Here we demonstrate that cable bacteria conduct electrons over centimetre distances via highly conductive fibres embedded in the cell envelope. Direct electrode measurements reveal nanoampere currents in intact filaments up to 10.1 mm long (>2000 adjacent cells). A network of parallel periplasmic fibres displays a high conductivity (up to 79 S cm(-1)), explaining currents measured through intact filaments. Conductance rapidly declines upon exposure to air, but remains stable under vacuum, demonstrating that charge transfer is electronic rather than ionic. Our finding of a biological structure that efficiently guides electrical currents over long distances greatly expands the paradigm of biological charge transport and could enable new bio-electronic applications. |
|
| |
Address |
|
|
| |
Corporate Author |
|
Thesis |
|
|
| |
Publisher |
|
Place of Publication |
|
Editor |
|
|
| |
Language |
|
Wos |
000485216900006 |
Publication Date |
2019-09-11 |
|
| |
Series Editor |
|
Series Title |
|
Abbreviated Series Title |
|
|
| |
Series Volume |
|
Series Issue |
|
Edition |
|
|
| |
ISSN |
2041-1723 |
ISBN |
|
Additional Links |
UA library record; WoS full record; WoS citing articles |
|
| |
Impact Factor |
12.124 |
Times cited |
10 |
Open Access |
|
|
| |
Notes |
; This research was financially supported by the European Research Council under the European Union's Seventh Framework Programme (FP/2007-2013) through ERC Grant 306933 (F.J.R.M.), the Research Foundation Flanders (FWO project grant G031416N), and the Netherlands Organisation for Scientific Research (VICI grant 016.VICI.170.072 to F.J.R.M.). H.J.E.B., C.J.B. and H.S.J.Z. were supported by the Netherlands Organisation for Scientific Research (NWO/OCW), as part of the Frontiers of Nanoscience program. R.B. is supported by an 'aspirant' grant from Research Foundation Flanders (FWO). We thank Laurine Burdorf (UAntwerpen) for help with Thiothrix cultivation, Marlies Nijemeisland (Faculty of Aerospace, TU Delft) for assistance with Raman microscopy, and Jan D'Haen (UHasselt) and Renaat Dasseville (UGent) for help with EM imaging. ; |
Approved |
Most recent IF: 12.124 |
|
| |
Call Number |
UA @ admin @ c:irua:162795 |
Serial |
5451 |
|
| Permanent link to this record |
