Title: Hemeprotein
Content: demand for energy. Therefore, muscle cells use myoglobin to accelerate oxygen diffusion and act as localized oxygen reserves for times of intense respiration. In vertebrates, hemoglobin is found in the cytosol of red blood cells in the bloodstream. Hemoglobin is sometimes referred to as the oxygen transport protein, in order to contrast it with its stationary cousin myoglobin, although its function and mechanism are more complex than this name would suggest. In vertebrates, oxygen is taken into the body by the tissues of the lungs, and passed to the red blood cells in the bloodstream. Oxygen is then distributed to

Title: Myoglobin
Content: by protein matrix that prevents close approach of the Fe-porphyrin assemblies. Myoglobin Myoglobin (symbol Mb or MB) is an iron- and oxygen-binding protein found in the muscle tissue of vertebrates in general and in almost all mammals. It is distantly related to hemoglobin which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells. In humans, myoglobin is only found in the bloodstream after muscle injury. It is an abnormal finding, and can be diagnostically relevant when found in blood. Myoglobin is the primary oxygen-carrying pigment of muscle tissues. High concentrations of myoglobin in muscle cells

Title: Hemoglobin
Content: blood. In mammals, the protein makes up about 96% of the red blood cells' dry content (by weight), and around 35% of the total content (including water). Haemoglobin has an oxygen-binding capacity of 1.34 mL O per gram, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules. Hemoglobin is involved in the transport of other gases: It carries some of the body's respiratory carbon dioxide (about 20–25% of the total) as carbaminohemoglobin, in which CO is bound to the heme protein. The molecule

Title: Hemocyanin
Content: Hemocyanin Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O). They are second only to hemoglobin in frequency of use as an oxygen transport molecule. Unlike the hemoglobin in red blood cells found in vertebrates, hemocyanins are not bound to blood cells but are instead suspended directly in the hemolymph. Oxygenation causes a color change between the colorless Cu(I) deoxygenated form and the blue Cu(II) oxygenated form. Hemocyanins are found only in the Mollusca and Arthropoda:

Title: Red blood cell
Content: Hemoglobin in the red blood cells also carries some of the waste product carbon dioxide back from the tissues; most waste carbon dioxide, however, is transported back to the pulmonary capillaries of the lungs as bicarbonate (HCO) dissolved in the blood plasma. Myoglobin, a compound related to hemoglobin, acts to store oxygen in muscle cells. The color of red blood cells is due to the heme group of hemoglobin. The blood plasma alone is straw-colored, but the red blood cells change color depending on the state of the hemoglobin: when combined with oxygen the resulting oxyhemoglobin is scarlet, and when

Question: What is the oxygen-carrying protein found in the red blood cells of the body?
Answer: Hemoglobin