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Published by: api-3807124 on Oct 17, 2008
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When we breathe in oxygen, the red blood cells transport it around to every cell inthe body – a critical process that has far-reaching evolutionary consequences. The adventof aerobic respiration, which added the oxygen-utilising tricarboxylic acid cycle andelectron transport system onto anaerobicglycolysis, allowed aerobic organisms to extract18 times more energy from glucose in the form of ATP. Initially, organisms relied ondiffusion to transport oxygen to their cells, an inefficient system that kept themmicroscopic in size. Then with the development of the body cavity came a primitivecirculatory system involving the flow of interstitial fluid through the action of muscular movement; yet, body size remained small, as this system of circulation was limited in itseffectiveness. Nematode worms have a primitive type of body cavity (pseudocoelom)and circulation; these tiny animals consist of just under a 1000 cells and as such are barely visible with the naked eye. With the advent of a true circulatory system totransport highly specialised red blood cells close to every cell in the body no matter howlarge the organism, so that oxygen could now reach all cells, body size was able toexpand radically up to the largest animal to currently inhabit the earth: the blue whale,which can weight up to 150 tons and stretch 100 feet in length from head to tail.
 Haemoglobin, an Oxygen Carrier 
A drop of blood contains millions of red bloodcells, or erythrocytes. These specialised cells are likeflattened discs, which gives them a much greater surfacearea with which to exchange oxygen and carbon dioxide inthe lungs and with body cells. Red blood cells are able tocarry oxygen so efficiently because of a special proteininside them: haemoglobin. In fact, it is the haemoglobinthat is responsible for the colour of the red blood cell. Haemoglobin contains a haem prosthetic group that has an iron atom at its centre. When the iron is bound to oxygen,the haem group is red in colour (oxyhameoglobin), and when it lacks oxygen(deoxygenated form) it is blue-red. As blood passes through the lungs, the haemoglobin picks up oxygen because of the increased oxygen pressure in the capillaries of the lungs,and can then release this oxygen to body cells where the oxygen pressure in the tissues islower. In addition, the red blood cells can pick up the waste product, carbon dioxide,some of which is carried by the haemoglobin (at a different site from where it carries theoxygen), while the rest is dissolved in the plasma. The high carbon dioxide levels in thetissues lowers the pH, and the binding of haemoglobin to carbon dioxide causes aconformational change that facilitates the release of oxygen. The carbon dioxide is thenreleased once the red blood cells reach the lungs.Haemoglobin is composed of four polypeptide chains, which in adults consist of two alpha () globin chains and two beta () globin chains (i.e. 22).
Each polypeptide has a haem prosthetic group attached, where each haem can bind one oxygen
Red blood cells
molecule - so there are four haem groups per haemoglobin molecule that together bindfour oxygen molecules.3-dimensional structure of hemoglobin. The four subunits are shown in redand yellow, and the heme groups in green.
(frequently abbreviated as
) is theiron-containingoxygen-transportmetalloproteinin thered cellsof the bloodinmammalsand other  animals. Hemoglobin in vertebrates transports oxygen from thelungsto the rest of the body, such as to themuscles, where it releases the oxygen load. Hemoglobin also has avariety of other gas-transport and effect-modulation duties, which vary from species tospecies, and which in invertebrates may be quite diverse.The name
is the concatenation of 
, reflecting the fact thateachsubunitof hemoglobin is aglobular proteinwith an embeddedheme(or haem) group; each heme group contains an iron atom, and this is responsible for the binding of oxygen. The most common types of hemoglobin contains four such subunits, each withone heme group.Mutations in thegenesfor the hemoglobin protein in humans result in a group of hereditary diseasestermed the
,the most common members of whicharesickle-cell diseaseandthalassemia. Historically in human medicine, hemaglobinopathies were the first diseases to be understood in mechanism of dysfunction, down to the molecular level.Hemoglobin is synthesized in the mitochondria of the immature red blood cell throughoutits early development from the proerythroblast to the reticulocyte in the bone marrow,when the nucleus has been lost. Even after the loss of the nucleus, residual ribosomal29
RNA allow further synthesis of Hb until the reticulocyte loses its RNA on entering thevasculature. Hemoglobin is chemically represented by (C
 Heme group
 The hemoglobinmoleculein humans is an assembly of four globular proteinsubunits. Eachsubunitis composed of a proteinchain tightly associated with a non-proteinheme  group.Each individual protein chain arranges in a set of alpha-helixstructural segmentsconnected together in aglobin foldarrangement, so called because this arrangement is thesame folding motif used in other heme/globin proteins such asmyoglobin. This folding pattern contains a pocket which is suitable to strongly bind the heme group.A heme group consists of an iron atom held in aheterocyclicring, known as a
.This iron atom is the site of oxygen binding. The iron atom is bonded equally to all four nitrogensin the center of the ring, which lie in one plane. Two additional bonds perpendicular to the plane on each side can be formed with the iron to a fifth and sixth bonding position, one connected strongly to the protein, the other available for binding of an oxygen molecule. The iron atom may either be in the Fe
or Fe
state, butferrihemoglobin (methemoglobin) (Fe
) cannot bind oxygen.The Fe
in hemoglobin may exist in either a high-spin (deoxygenated) or low-spin(oxygenated) state, according to population of the iron (II) d-orbital structure with its 6available d electrons, as understood incrystal field theory. With the binding of an oxygenmolecule as a sixth ligand to iron, the iron (II) atom finds itself in a
octahedral field 
(defined by the
ligand points of the four porphyrin ring nitrogens, the histamine30

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