title: Oxygen, oxidases, and the essential trace metals.
abstract: The dominant function of dioxygen as the terminal electron acceptor in aerobic systems is well established; the roles of iron and copper in the terminal oxidases are less well understood. The minor, but crucial, part that dioxygen plays in other biological processes has recently attracted much attention. The chemistry of the reduction products of dioxygen is described and the possible relation of these products to the toxic properties of dioxygen is discussed. It is suggested that the uncontrolled reaction of dioxygen with reduced species, to give the superoxide ion, hydrogen peroxide, the hydroxyl radical and perhaps other entities derived from these, is potentially hazardous to the organism. Defences exist against these species, not least in the dismutases dependent on copper-zinc, manganese and iron, in catalase and in the selenium-dependent peroxidase. The effectiveness of these defences is examined and their reduction products of dioxygen during phagocytosis is discussed.
mesh_terms: D003300:Copper / Q000502:physiology; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000502:physiology*; D005609:Free Radicals; D005979:Glutathione Peroxidase / Q000502:physiology; D007501:Iron / Q000502:physiology; D010084:Oxidation-Reduction; D010100:Oxygen / Q000502:physiology*; D010544:Peroxidases / Q000502:physiology*; D010587:Phagocytosis; D013482:Superoxide Dismutase / Q000502:physiology*; D014131:Trace Elements / Q000502:physiology*; D015032:Zinc / Q000502:physiology
chemical_list: D005609:Free Radicals; D014131:Trace Elements; D003300:Copper; D007501:Iron; D010544:Peroxidases; D005979:Glutathione Peroxidase; D013482:Superoxide Dismutase; D003576:Electron Transport Complex IV; D015032:Zinc; D010100:Oxygen