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Pyrroloquinoline quinone redox potential

Willner et al. [52] have created some elegant interfacial supramolecular assemblies to address this issue by removing the non-covalently bound flavin adenine dinucleotide (FAD) redox center from glucose oxidase and immobilizing the enzyme on a tether consisting of cystamine chemisorbed on a gold surface, a pyrroloquinoline quinone (PQQ) link and FAD. The mediator potential and electron transfer distances of this assembly were carefully chosen so that transfer of electrons from the FAD to the PQQ and to the electrode is very fast. A maximum rate of 900 150 s-1 for the enzymatic reaction within this monolayer assembly was obtained, which is indistinguishable from the value of about 1000 s-1 obtained for the enzyme in solution. While monolayers can offer molecular-level control of the interfacial structure, the... [Pg.193]

In Chap. 3, redox-active c-conjugated systems allow us to construct a variety of potential redox catalysts and electronic materials. A coenzyme PQQ possessing the t-conjugated pyrroloquinoline quinone function, serves as a catalyst or mediator in redox reactions under molecular oxygen. [Pg.3]


See other pages where Pyrroloquinoline quinone redox potential is mentioned: [Pg.45]    [Pg.563]    [Pg.148]    [Pg.90]    [Pg.45]    [Pg.317]    [Pg.397]   
See also in sourсe #XX -- [ Pg.574 ]




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