Mb (a monomer containing 8 a-helices, A-H) and Hb (a heterotetramer with two a -and two b-subunits, each which also contains 8 a-helices) are both oxygen binding proteins. Dioxygen is transported from lungs, gills, or skin of an animal to capillaries, where it can be delivered to respiring tissue. It has a low solubility in blood (0.1 mM). Whole blood, which contains 150 g Hb/L, and can carry up to 10 mM dioxygen. Invertebrate can have alternative proteins for oxygen binding, including hemocyanin, which contains Cu and hemerythrin, a non-heme protein. On binding dioxygen, solutions of Hb change color to bright red. Solutions of hemocyanin and hemerythrin change to blue and burgundy colored, respectively, on binding dioxygen. Some Antarctic fish don't require Hb since dioxygen is more soluble at low temperature. Mb is found in the muscle, and serves as a storage protein for oxygen transported by Hb.