Current Projects: Flavoenzyme oxidases

Hundreds of enzymes have been identified that utilize a flavin cofactor to create a reactive center.  The functional group of a flavin, the 7,8-dimethylisoalloxazine is a highly versatile molecule which, depending on its environment, can serve as a donor or acceptor of one or two electrons.  This versatility of the flavin makes it an ideal catalyst for a variety of reactions, including dehydrogenation, oxidation, reduction, electron transfer, bioluminescence and more.


7,8-dimethylisoalloxazine moiety of a flavin cofactor

The flavoenzyme creates a specific microenvironment around the flavin and modulates the flavin's activity to produce a desired outcome.  The relationship between flavoprotein structure and function are complex and not well understood.  Often, flavoenzymes of similar general fold catalyze entirely different reactions, while flavoenzymes that greatly differ in structure may have highly similar functions.  In the Vrielink lab, we have chosen three flavoenzyme oxidases to study the relationship between flavoprotein structure and function.  Each of these enzymes uniquely contributes to our understanding of flavoenzyme structure and catalysis.

      L-amino acid oxidase
      Cholesterol oxidase (Brevibacterium sterolicum, covalently attached FAD)
      Cholesterol oxidase (Streptomyces sp., non-covalently attached FAD)
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