Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Arjen J. J. Olsthoorn"'
Publikováno v:
European Journal of Biochemistry. 247:659-665
To investigate the mode of binding and the role of Ca2+ in soluble, pyrroloquinoline-quinone (PQQ)-containing glucose dehydrogenase of the bacterium Acinetobacter calcoaceticus (sGDH), the following enzyme species were prepared and their interconvers
Publikováno v:
Journal of Electroanalytical Chemistry. 368:165-171
A gold electrode surface was modified with a chemisorbed monolayer of cystamine, and the cystamine amino groups were used for covalent immobilization of pyrroloquinoline quinone (PQQ). The spacer length between the electrode surface and the immobiliz
Autor:
Wolfgang Schuhmann, Arjen J. J. Olsthoorn, Adam Heller, Johannis A. Duine, Martin. Haemmerle, Ling Ye, Hans Ludwig. Schmidt
Publikováno v:
Analytical Chemistry. 65:238-241
Glucose electrodes were prepared by wiring quinoprotein glucose dehydrogenase, GDH (EC 1.1.99.17) to glassy carbon with an osmium complex containing redox-conducting epoxy network. Their current density at 70 mM glucose concentration reached 1.8 mA c
Autor:
Arjen J. J. Olsthoorn, Kor H. Kalk, Henriëtte J. Rozeboom, Johannis A. Duine, Arthur Oubrie, Bauke W. Dijkstra
Publikováno v:
Journal of Molecular Biology, 292(19), 5187-5194. Academic Press
Soluble glucose dehydrogenase (s-GDH; EC 1.1.99.17) is a classical quinoprotein which requires the cofactor pyrroloquinoline quinone (PQQ) to oxidize glucose to gluconolactone. The reaction mechanism of PQQ-dependent enzymes has remained controversia
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::70802eeba82f3863802434ba3d9e68be
https://research.rug.nl/en/publications/47904af5-dca4-4c0b-a12f-3b00f5a1f337
https://research.rug.nl/en/publications/47904af5-dca4-4c0b-a12f-3b00f5a1f337
Publikováno v:
Biochemistry. 37(39)
Kinetic and optical studies were performed on the reductive half-reaction of soluble, quinoprotein glucose dehydrogenase (sGDH), i.e., on the conversion of sGDHox plus aldose sugar into sGDHred plus corresponding aldonolactone. It appears that the na
Publikováno v:
European journal of biochemistry. 255(1)
Steady-state-kinetics investigations were carried out for the oxidation of aldose sugars by soluble quinoprotein glucose dehydrogenase (GDH) from Acinetobacter calcoaceticus using N-methylphenazonium methyl sulfate (PMS) as artificial electron accept
Publikováno v:
Archives of biochemistry and biophysics. 336(1)
Soluble, periplasmic quinoprotein glucose dehydrogenase of Acinetobacter calcoaceticus (sGDH; EC 1.1.99.17) was produced in good yield in the apoenzyme form (without the cofactor pyrroloquinoline quinone, PQQ) by an Escherichia coli recombinant strai
Publikováno v:
European Journal of Biochemistry. Jul98 Part 1, Vol. 255 Issue 1, p255-261. 7p. 1 Diagram, 1 Chart, 10 Graphs.
Autor:
Wayne Burleson, Sandro Carrara
This book presents a systematic approach to analyzing the challenging engineering problems posed by the need for security and privacy in implantable medical devices (IMD). It describes in detail new issues termed as lightweight security, due to the a