Structural methods for probing the interaction of flavoenzymes with dioxygen and its surrogates
2019
Abstract As a rare feature among organic cofactors, reduced flavins (Fl red ) can efficiently react with dioxygen (O 2 ). As a consequence, many flavin-dependent enzymes may serve as either oxidases that use O 2 as an electron acceptor or as monooxygenases that transfer one oxygen atom derived from O 2 to an organic substrate. For the latter functionality, covalent flavin: oxygen adducts are formed that function as oxygenating species. Remarkably, despite intensive research, many open questions remain how flavoenzymes control the reaction with O 2 . Here, we describe O 2 -pressurized protein crystallography in detail as a structural approach to gain insight into the interactions between the protein scaffold, the flavin cofactor and O 2 . This may allow to further our understanding of how flavoenzymes can steer the formation of different oxygenating species and thus provide missing puzzle pieces for rational flavoenzyme design.
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