Many biochemical processes exploit the extraordinary versatility of flavoen
zymes and their flavin cofactors, Flavoproteins are now known to have a var
iety of folding topologies but a careful examination of their structures su
ggests that there are recurrent features in their catalytic apparatus. The
flavoenzymes that catalyse dehydrogenation reactions share a few invariant
features in the hydrogen-bond interactions between their protein and flavin
constituents. Similarly, the positioning of the reactive part of the subst
rate with respect to the cofactor is generally conserved. Modulation of sub
strate and cofactor reactivity and exact positioning of the substrate are k
ey elements in the mode of action of these enzymes.