Blood
About 98.5% of the oxygen in a sample of arterial blood in a healthy human breathing air at sea-level pressure is chemically combined with the hemoglobin. About 1.5% is physically dissolved in the other blood liquids and not connected to hemoglobin. The hemoglobin molecule is the primary transporter of oxygen in mammals and many other species (for exceptions, see below). Hemoglobin has an oxygen binding capacity between 1.36 and 1.40 ml O per gram hemoglobin, which increases the total blood oxygen capacity seventyfold, compared to if oxygen solely were carried by its solubility of 0.03 ml O per liter blood per mm Hg partial pressure of oxygen (about 100 mm Hg in arteries).
Oxygen toxicity
The biochemical basis for the toxicity of oxygen is the partial reduction of oxygen by one or two electrons to form reactive oxygen species, which are natural by-products of the normal metabolism of oxygen and have important roles in cell signalling. One species produced by the body, the superoxide anion (), is possibly involved in iron acquisition. Higher than normal concentrations of oxygen lead to increased levels of reactive oxygen species. Oxygen is necessary for cell metabolism, and the blood supplies it to all parts of the body. When oxygen is breathed at high partial pressures, a hyperoxic condition will rapidly spread, with the most vascularised tissues being most vulnerable. During times of environmental stress, levels of reactive oxygen species can increase dramatically, which can damage cell structures and produce oxidative stress.