To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes.
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.
Mattevi
Andrea
A
Department of Genetics and Microbiology, University of Pavia, via Ferrata 1, Pavia 27100, Italy. mattevi@ipvgen.unipv.it
D004798:Enzymes / Q000737:chemistry / Q000378:metabolism*; D005415:Flavins / Q000378:metabolism*; D005420:Flavoproteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D010088:Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism*
D004798:Enzymes; D005415:Flavins; D005420:Flavoproteins; D010088:Oxidoreductases; D010100:Oxygen