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Flavin-dependent enzymes catalyse a wide range of reactions and, thereby, facilitate a variety of cellular processes. Among the properties that equip flavoenzymes with this chemical versatility is their reactivity towards oxygen, which shows huge variation among flavoproteins. A survey of known 3D structures of flavin-dependent oxidases and dehydrogenases and the correlation with their functional properties indicates that there are no structural rules that enable prediction of whether or how a flavoenzyme reacts with oxygen. Combinations of subtle factors such as dipole pre-organization, charge distribution, dynamics and solvation in the active centre determine the balance of interactions that control oxygen reactivity. The chemical basis of oxygen reactivity remains a puzzling problem and represents one of the challenging questions in modern flavoenzymology. [Copyright &y& Elsevier]

Deals with the comment of Scott Dick, et al, on a study on flavin-dependent N-hydroxylating enzymes. Putative flavin adenine dinucleotide (FAD)-binding site of lysine N-hydroxylase; Features of the proposed FAD-binding site.

Deals with the cofactor- and substrate-binding domains in flavin-dependent N-hydroxylating lucD enzyme. Details on studies on lucD; Description on the soluble form of lucD; Construction of different plasmids which encode modified lucD forms (rlucDs).