Structural Modification of PQQ and its Effect on the Reconstitution of the 'Holo'enzyme and Catalytic Activity.
Adah Almutairi
Faculty Advisor: Tetsuo Otsuki

     Discovered in 1979, PQQ pyrroloquinoline quinone) is known to be an essential cofactor in some methanol and glucose dehydrogenase systems. PQQ has been found to have active redox sites as well as binding sites to Ca²⁺ and the apoprotein. The systematic reconstitution study of 'holo'enzyme with our PQQ analogs will give us better insight into PQQ's binding sites and increase understanding of its redox characteristics in the reconstituted enzyme. These analogs will serve as isosteric probes to reveal how PQQ binds to the active sites of PQQ-requiring quinoproteins such as soluble glucose dehydrogenase. In our study we synthesize three PQQ analogs, each differing from each other and PQQ in the location of the N-atoms. Careful systematic analysis of the results will shed more light on the enzymatic characteristics of soluble glucose dehydrogenase.