Both hemoglobin and myoglobin contain a prosthetic group called heme, which contains a central iron (Fe) atom. By itself, heme is not a good oxygen carrier: it must be part of a larger protein to prevent oxidation of the iron. The heme prosthetic group is entirely buried within myoglobin. Each iron atom can form six coordination bonds. Two of these bonds are formed between iron and oxygen. Each hemoglobin or myoglobin molecule can bind four oxygen molecules. Hemoglobin is a heterotetramer, whereas myoglobin is a monomer. Molecular oxygen binds reversibly to the Fe(II) atom in heme.