Quinone-Modified Surfaces for Enhanced Enzyme-Electrode Interactions in Pyrroloquinoline-Quinone-Dependent Glucose Dehydrogenase Anodes

2014 ◽  
Vol 1 (11) ◽  
pp. 2017-2028 ◽  
Author(s):  
Sofia Babanova ◽  
Ivana Matanovic ◽  
Plamen Atanassov
Keyword(s):  
Glucose Dehydrogenase ◽  
Pyrroloquinoline Quinone ◽  
Enzyme Electrode ◽  
Modified Surfaces

scholarly journals Screening of Peptide Ligands for Pyrroloquinoline Quinone Glucose Dehydrogenase Using Antagonistic Template-Based Biopanning

2013 ◽  
Vol 14 (12) ◽  
pp. 23244-23256 ◽  
Author(s):  
Koichi Abe ◽  
Wataru Yoshida ◽  
Kotaro Terada ◽  
Yukiko Yagi-Ishii ◽  
Stefano Ferri ◽  
...  
Keyword(s):  
Glucose Dehydrogenase ◽  
Pyrroloquinoline Quinone ◽  
Peptide Ligands

scholarly journals Identification of Pantoea ananatis gene encoding membrane pyrroloquinoline quinone (PQQ)-dependent glucose dehydrogenase and pqqABCDEF operon essential for PQQ biosynthesis

2011 ◽  
Vol 318 (1) ◽  
pp. 55-60 ◽  
Author(s):  
Irina G. Andreeva ◽  
Lyubov I. Golubeva ◽  
Tatiana M. Kuvaeva ◽  
Evgueni R. Gak ◽  
Joanna I. Katashkina ◽  
...  
Keyword(s):  
Glucose Dehydrogenase ◽  
Pyrroloquinoline Quinone ◽  
Pantoea Ananatis ◽  
Gene Encoding ◽  
Pqq Biosynthesis

Ca2+ stabilizes the semiquinone radical of pyrroloquinoline quinone

2001 ◽  
Vol 357 (3) ◽  
pp. 893-898 ◽  
Author(s):  
Akihiro SATO ◽  
Kazuyoshi TAKAGI ◽  
Kenji KANO ◽  
Nobuo KATO ◽  
Johannis A. DUINE ◽  
...  
Keyword(s):  
Redox Potential ◽  
Active Site ◽  
Continuous Flow ◽  
Glucose Dehydrogenase ◽  
Acinetobacter Calcoaceticus ◽  
Substrate Oxidation ◽  
Pyrroloquinoline Quinone ◽  
Free State ◽  
Semiquinone Radical ◽  
Chemical Mechanisms

Spectroelectrochemical studies were performed on the interaction between Ca2+ and pyrroloquinoline quinone (PQQ) in soluble glucose dehydrogenase (sGDH) and in the free state by applying a mediated continuous-flow column electrolytic spectroelectrochemical technique. The enzyme forms used were holo-sGDH (the holo-form of sGDH from Acinetobacter calcoaceticus) and an incompletely reconstituted form of this, holo-X, in which the PQQ-activating Ca2+ is lacking. The spectroelectrochemical and ESR data clearly demonstrated the generation of the semiquinone radical of PQQ in holo-sGDH and in the free state in the presence of Ca2+. In contrast, in the absence of Ca2+ no semiquinone was observed, either for PQQ in the free state (at pH7.0) or in the enzyme (holo-X). Incorporation of Ca2+ into the active site of holo-X, yielding holo-sGDH, caused not only stabilization of the semiquinone form of PQQ but also a negative shift (of 26.5mV) of the two-electron redox potential, indicating that the effect of Ca2+ is stronger on the oxidized than on the reduced PQQ. Combining these data with the observations on the kinetic and chemical mechanisms, it was concluded that the strong stimulating effect of Ca2+ on the activity of sGDH can be attributed to facilitation of certain kinetic steps, and not to improvement of the thermodynamics of substrate oxidation. The consequences of this conclusion are discussed for the oxidative as well as for the reductive part of the reaction of sGDH.

scholarly journals Amino Acid Residues Interacting with Both the Bound Quinone and Coenzyme, Pyrroloquinoline Quinone, inEscherichia coliMembrane-bound Glucose Dehydrogenase

2008 ◽  
Vol 283 (32) ◽  
pp. 22215-22221 ◽  
Author(s):  
Golam Mustafa ◽  
Yoshinori Ishikawa ◽  
Kazuo Kobayashi ◽  
Catharina T. Migita ◽  
M. D. Elias ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glucose Dehydrogenase ◽  
Pyrroloquinoline Quinone ◽  
Amino Acid Residues
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