Zobrazeno 1 - 7
of 7
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