3-dimensional structure of hemoglobin. The four subunits are shown in red and yellow, and the heme groups in green.

Hemoglobin or haemoglobin (frequently abbreviated as Hb) is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals. Hemoglobin transports oxygen from the lungs to the rest of the body, such as to the muscles, where it releases the oxygen load. hemoglobin visualization, provided by user:Kku, rendered by Cn3D, File history Legend: (cur) = this is the current file, (del) = delete this old version, (rev) = revert to this old version. ... hemoglobin visualization, provided by user:Kku, rendered by Cn3D, File history Legend: (cur) = this is the current file, (del) = delete this old version, (rev) = revert to this old version. ... General Name, Symbol, Number iron, Fe, 26 Chemical series transition metals Group, Period, Block 8, 4, d Appearance lustrous metallic with a grayish tinge Atomic mass 55. ... General Name, Symbol, Number oxygen, O, 8 Chemical series Nonmetals Group, Period, Block 16, 2, p Appearance colorless Atomic mass 15. ... In biochemistry, a metalloprotein is a generic term for a protein that also contains a metal cofactor. ... Human red blood cells Red blood cells are the most common type of blood cell and are the vertebrate bodys principal means of delivering oxygen from the lungs or gills to body tissues via the blood. ... Human blood smear: a - erythrocytes; b - neutrophil; c - eosinophil; d - lymphocyte. ... Orders Subclass Multituberculata (extinct) Plagiaulacida Cimolodonta Subclass Palaeoryctoides (extinct) Subclass Triconodonta (extinct) Subclass Eutheria (includes extinct ancestors)/Placentalia (excludes extinct ancestors) Afrosoricida Artiodactyla Carnivora Cetacea Chiroptera Cimolesta (extinct) Creodonta (extinct) Condylarthra (extinct) Dermoptera Desmostylia (extinct) Embrithopoda (extinct) Hyracoidea Insectivora Lagomorpha Litopterna (extinct) Macroscelidea Mesonychia (extinct) Notoungulata (extinct) Perissodactyla Pholidota Plesiadapiformes... The lungs flank the heart and great vessels in the chest cavity. ... A top-down view of skeletal muscle Muscle is the contractile tissue of the body and is derived from the mesodermal layer of embryonic germ cells. ...

The name hemoglobin is the concatenation of heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme (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. In structural biology, a protein subunit or subunit protein is a single protein molecule that assembles (or coassembles) with other protein molecules to form a multimeric or oligomeric protein. ... Globular proteins, or spheroproteins are one of the two main protein classes, comprising globelike proteins that are more or less soluble in aqueous solutions (where they form colloidal solutions). ... Structure of Heme b A haem or heme is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. ...

Mutations in the gene for the hemoglobin protein result in a group of hereditary diseases termed the hemoglobinopathies, the most common members of which are sickle-cell disease and thalassemia. This stylistic schematic diagram shows a gene in relation to the double helix structure of DNA and to a chromosome (right). ... A genetic disorder, or genetic disease is a disease caused, at least in part, by the genes of the person with the disease. ... Hemoglobinopathy is a kind of genetic defect that results in abnormal structure of one of the globin chains of the hemoglobin molecule. ... Sickle-shaped red blood cells Sickle cell disease is a general term for a group of genetic disorders caused by sickle hemoglobin (Hgb S). ... Thalassemia (American English) (or Thalassaemia in British English) is an inherited disease of the red blood cells, classified as a hemoglobinopathy. ...

Structure

Heme group

The Hemoglobin molecule is an assembly of four globular protein subunits. Each subunit is composed of a protein chain tightly associated with a non-protein heme group. Heme, by myself File links The following pages link to this file: Hemoglobin Heme Categories: GFDL images ... In general, a molecule is the smallest particle of a pure chemical substance that still retains its composition and chemical properties. ... Globular proteins, or spheroproteins are one of the two main protein classes, comprising globelike proteins that are more or less soluble in aqueous solutions (where they form colloidal solutions). ... In structural biology, a protein subunit or subunit protein is a single protein molecule that assembles (or coassembles) with other protein molecules to form a multimeric or oligomeric protein. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Structure of Heme b A haem or heme is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. ...

Each individual protein chain arranges in a set of alpha-helix structural segments connected together in a "myoglobin fold" arrangement, so called because this arrangement is the same folding motif used in the heme/globin proteins. This folding pattern contains a pocket which is suitable to strongly bind the heme group. A diagram of the alpha helix structure of amino acids In proteins, the α helix is a major structural motif in secondary structure. ... Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. ...

A heme group consists of an iron atom held in a heterocyclic ring, known as a porphyrin. This iron atom is the site of oxygen binding. The iron atom is bonded equally to all four nitrogens in 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 form the fifth and sixth positions, one connected strongly to the protein, the other available for binding of oxygen. The iron atom can either be in the Fe²⁺ or Fe³⁺ state, but ferrihaemoglobin (Methaemoglobin) (Fe³⁺) cannot bind oxygen. Heterocyclic compounds are substances which contain a ring structure as found in benzene and the aromatic compounds, or aromatic hydrocarbons, but in which other atoms than carbon, such as sulfur, oxygen or nitrogen are found as part of the ring. ... A porphyrin is a heterocyclic macrocycle made from 3 pyrrole subunits and one pyrroline subunit, and linked on opposite sides through 4 methine bridges. ... General Name, Symbol, Number nitrogen, N, 7 Chemical series nonmetals Group, Period, Block 15, 2, p Appearance colorless Atomic mass 14. ... Methaemoglobin is a form of the oxygen-carrying protein haemoglobin (also spelt hemoglobin), in which the iron in the haem group is in the Fe3+ state, not the Fe2+ of normal haemoglobin. ...

In adult humans, the most common hemoglobin type is a tetramer (which contains 4 subunit proteins) called hemoglobin A, consisting of two α and two β subunits non-covalently bound. This is denoted as α₂β₂. The subunits are structurally similar and about the same size. Each subunit has a molecular weight of about 16,000 daltons, for a total molecular weight of the tetramer of about 64,000 daltons. Haemoglobin A is the most intensively studied of the haemoglobin molecules. A tetramer is a protein with four subunits (tetrameric). ... The unified atomic mass unit (u), or dalton (Da), is a small unit of mass used to express atomic masses and molecular masses. ... The molecular mass of a substance (less accurately called molecular weight and abbreviated as MW) is the mass of one molecule of that substance, relative to the unified atomic mass unit u (equal to 1/12 the mass of one atom of carbon-12). ...

The four polypeptide chains are bound to each other by salt bridges, hydrogen bonds and hydrophobic interaction. There are two kinds of contacts between the α and β chains: α₁β₁ and α₁β₂. Peptides (from the Greek πεπτος, digestable), are the family of molecules formed from the linking, in a defined order, of various amino acids. ... In protein chemistry, the term salt bridge or salt bond is used to denote chemical bonds between positively and negatively charged side-chains of proteins. ... In chemistry, a hydrogen bond is a type of attractive intermolecular force that exists between two partial electric charges of opposite polarity. ... Hydrophobe (from the Greek (hydros) water and (phobos) fear) in chemistry refers to the physical property of a molecule that is repelled by water. ...

Types of haemoglobins in humans

In the embryo: Embryos (and one tadpole) of the wrinkled frog (Rana rugosa). ...

• Gower 1 (ξ₂ε₂)
• Gower 2 (α₂ε₂) (PDB 1A9W)
• Haemoglobin Portland (ξ₂γ₂)

In the fetus: The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. ... Fetus at eight weeks Foetus redirects here. ...

• Haemoglobin F (α₂γ₂) (PDB 1FDH)

In adults: Fetal hemoglobin protein structure Fetal hemoglobin (also hemoglobin F or HbF) is the main oxygen transport protein in the fetus during the last seven months of development in the womb. ... The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. ...

• Haemoglobin A (α₂β₂) (PDB 1BZ0) - The most common type.
• Haemaglobin A₂ (α₂δ₂) - δ chain synthesis begins late in the third trimester and in adults, it has a normal level of 2.5%
• Haemoglobin F (α₂γ₂) - In adults Haemoglobin F is restricted to a limited population of red cells called F cells.

The Protein Data Bank (PDB) is a repository for 3-D structural data of proteins and nucleic acids. ... Fetal hemoglobin protein structure Fetal hemoglobin (also hemoglobin F or HbF) is the main oxygen transport protein in the fetus during the last seven months of development in the womb. ...

Binding of ligands

In the tetrameric form of normal adult hemoglobin, the binding of oxygen is a cooperative process. The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule. As a consequence, the oxygen binding curve of hemoglobin is sigmoidal, or 'S'-shape, as opposed to the normal hyperbolic (noncooperative) curve. This positive cooperative binding is achieved through steric conformational changes of the hemoglobin protein complex: When one subunit protein in hemoglobin becomes oxygenated, it induces a confirmation or structural arrangement change in the whole complex causing the other three subunits to gain an increased affinity for oxygen. animation of hemoglobin t-r state transformation, home made. ... In biochemistry, a macromolecule has cooperative binding if when binding a ligand, the affinity of the ligand for the molecule changes depending on the amount of ligand already bound. ... Steric effects are the interaction of molecules dictated by their shape and/or spatial relationships. ...

Hemoglobin's affinity for oxygen is decreased in the presence of carbon monoxide because both gases compete for the same binding sites on hemoglobin, carbon monoxide binding preferentially to oxygen. Carbon dioxide occupies a different binding site on the hemoglobin. Carbon dioxide reacts with water to give bicarbonate, carbonic acid freed protons via the reaction, which is catalyzed by carbonic anhydrase: Carbon monoxide, chemical formula CO, is a colorless, odorless, tasteless, flammable and highly toxic gas. ... In inorganic chemistry, a bicarbonate (IUPAC-recommended nomenclature: hydrogencarbonate) is an intermediate form in the deprotonation of carbonic acid. ... Carbonic acid is a carbon-containing acid with the formula H2CO3. ... Carbonic anhydrase (carbonate dehydratase) is a family of zinc-containing enzymes that catalyze the rapid interconversion of carbon dioxide and water into carbonic acid, protons, and bicarbonate ions. ...

CO₂ + H₂O <-> HCO₃^- + H⁺

Hemoglobin sigmoidal oxygen dissociation curve

So blood with high carbon dioxide levels is also lower in pH (more acidic). Hemoglobin can bind protons and carbon dioxide which causes a conformational change in the protein and facilitates the release of oxygen. Protons bind at various places along the protein and carbon dioxide binds at the alpha-amino group forming carbamate. Conversely, when the carbon dioxide levels in the blood decrease (i.e., around the lungs), carbon dioxide is released, increasing the oxygen affinity of the protein. This control of hemoglobin's affinity for oxygen by the binding and release of carbon dioxide is known as the Bohr effect. Hemoglobin oxygen dissociation curve, drawn by User:Diberri in Adobe Illustrator. ... Hemoglobin oxygen dissociation curve, drawn by User:Diberri in Adobe Illustrator. ... The correct title of this article is pH. The initial letter is capitalized due to technical restrictions. ... For alternative meanings see acid (disambiguation). ... Properties In physics, the proton (Greek proton = first) is a subatomic particle with an electric charge of one positive fundamental unit (1. ... Carbamates are a group of organic compounds sharing a common functional group with the general structure -NH(CO)O-. More precisely the carbamate group is considered an amide group with an alkoxy or hydroxy functional group next to the carbonyl group. ... The Bohr effect is an adaption in animals to reduce the affinity of hemoglobin for oxygen as a response to an increase in blood carbon dioxide levels and a decrease in pH. It was first described by the Danish physiologist Christian Bohr in 1904. ...

The binding of oxygen is affected by molecules such as carbon monoxide (CO) (for example from tobacco smoking, cars and furnaces). CO competes with oxygen at the heme binding site. Hemoglobin binding affinity for CO is 200 times greater than its affinity for oxygen, meaning that small amounts of CO dramatically reduces hemoglobin’s ability to transport oxygen. When hemoglobin combines with CO, it forms a very bright-red compound called carboxyhemoglobin. When inspired air contains CO levels as low as 0.02% headache and nausea occur; if the CO concentration is increased to 0.1%, unconsciousness will follow. In heavy smokers, up to 20% of the oxygen-active sites can be blocked by CO. Carbon monoxide, chemical formula CO, is a colorless, odorless, tasteless, flammable and highly toxic gas. ... Various smoking equipment including different pipes, and cigars. ... Carboxyhemoglobin (COHb) is a stable complex of carbon monoxide and hemoglobin that forms in red blood cells when carbon monoxide is inhaled, and hinders delivery of oxygen to the body. ...

Hemoglobin also has competitive binding affinity for sulfur monoxide (SO), nitrogen dioxide (NO₂) and hydrogen sulfide (H₂S). The iron atom in the heme group must be in the Fe⁺² oxidation state to support oxygen transport. Oxidation to Fe⁺³ state converts hemoglobin into hemiglobin or methemoglobin which cannot bind oxygen. Nitrogen dioxide and nitrous oxide are capable of converting hemoglobin to methemoglobin. In chemistry, Sulfur monoxide (formula: SO) is an unstable species that forms when monatomic oxygen O reacts with sulfur S2. ... The chemical compound nitrogen dioxide (NO2) is a red or orange/brown gas with a characteristic sharp, biting odor. ... Hydrogen sulfide (hydrogen sulphide in British English), H2S, is a colorless, toxic, flammable gas that is responsible for the foul odor of rotten eggs. ... Methemoglobin (also hemiglobin) is a type of hemoglobin that is produced by the oxidation of the ferrous iron contained in hemoglobin to ferric iron which doesnt have the capacity for carrying oxygen. ... Nitrous oxide, also known as dinitrogen oxide or dinitrogen monoxide, is a chemical compound with chemical formula N2O. Under room conditions, it is a colourless non-flammable gas, with a pleasant, slightly-sweet odor. ...

In people acclimated to high altitudes, the concentration of 2,3-bisphosphoglycerate (2,3-BPG) in the blood is increased, which allows these individuals to deliver a larger amount of oxygen to tissues under conditions of lower oxygen tension. This phenomenon, where molecule Y affects the binding of molecule X to a transport molecule Z, is called a heterotropic allosteric effect. In biochemistry, an enzyme or other protein is allosteric if its activity or efficiency changes in response to the binding of an effector molecule at a so-called allosteric site. ...

A variant hemoglobin, called fetal hemoglobin (Hb F, α₂γ₂), is found in the developing fetus, and binds oxygen with greater affinity than adult hemoglobin. This means that the oxygen binding curve for fetal hemoglobin is left-shifted (i.e., a higher percentage of hemoglobin has oxygen bound to it at lower oxygen tension), in comparison to that of adult hemoglobin. As a result, fetal blood in the placenta is able to take oxygen from maternal blood. Fetal hemoglobin protein structure Fetal hemoglobin (also hemoglobin F or HbF) is the main oxygen transport protein in the fetus during the last seven months of development in the womb. ... Fetus at eight weeks Foetus redirects here. ... The placenta is an ephemeral and temporary organ present only in female placental mammals during gestation (pregnancy). ...

Degradation of hemoglobin

When red cells reach the end of their life due to aging or defects, they are broken down, and the hemoglobin molecule broken up and the iron recycled. When the porphyrin ring is broken up, the fragments are normally secreted in the bile by the liver. The major final product of heme degradation is bilirubin. Increased levels of this chemical are detected in the blood if red cells are being destroyed more rapidly than usual. Improperly degraded hemoglobin protein or hemoglobin that has been released from the blood cells can clog small blood vessels, especially the delicate blood filtering vessels of the kidneys, causing kidney damage. Red Teams or Red Cells are U.S. government parlance for teams or units designed to test the effectiveness of U.S. tactics or personnel. ... Bile (or gall) is a bitter, greenish-yellow alkaline fluid secreted by the liver of most vertebrates. ... The liver is one of the largest internal organs of the human body. ... Bilirubin is a yellow breakdown product of haem (heme in American English). ... Human kidneys viewed from behind with spine removed The kidneys are bean-shaped excretory organs in vertebrates. ...

Role in disease

Decreased levels of hemoglobin, with or without an absolute decrease of red blood cells, leads to symptoms of anemia. Anemia has many different causes, although iron deficiency and its resultant iron deficiency anemia are the most common causes in the Western world. As absence of iron decreases heme synthesis, red blood cells in iron deficiency anemia are hypochromic (lacking the red hemoglobin pigment) and microcytic (smaller than normal). Other anemias are rarer. In hemolysis (accelerated breakdown of red blood cells), associated jaundice is caused by the hemoglobin metabolite bilirubin, and the circulating hemoglobin can cause renal failure. Human red blood cells Red blood cells are the most common type of blood cell and are the vertebrate bodys principal means of delivering oxygen from the lungs or gills to body tissues via the blood. ... This article discusses the medical condition. ... // Introduction Iron deficiency is the most common known form of nutritional deficiency. ... Iron deficiency anemia is the most common type of anemia, and the most common cause of microcytic anemia. ... Structure of Heme b A haem or heme is a prosthetic group that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin. ... Hemolysis (alternative spelling haemolysis) is the excessive breakdown of red blood cells. ... Jaundice, also known as icterus (adjective:Icteric), is yellowing of the skin, sclera (the white of the eyes) and mucous membranes caused by increased levels of bilirubin in the human body. ... Bilirubin is a yellow breakdown product of haem (heme in American English). ... Renal failure is the condition where the kidneys fail to function properly. ...

Mutations in the globin chain are associated with the hemoglobinopathies, such as sickle-cell disease and thalassemia. Hemoglobinopathy is a kind of genetic defect that results in abnormal structure of one of the globin chains of the hemoglobin molecule. ... Sickle-shaped red blood cells Sickle cell disease is a general term for a group of genetic disorders caused by sickle hemoglobin (Hgb S). ... Thalassemia (American English) (or Thalassaemia in British English) is an inherited disease of the red blood cells, classified as a hemoglobinopathy. ...

There is a group of genetic disorders, known as the porphyrias that are characterized by errors in metabolic pathways of heme synthesis. King George III of the United Kingdom was probably the most famous porphyria sufferer. This article is about the disease. ... George III (George William Frederick) (4 June 1738 – 29 January 1820) was King of Great Britain, and King of Ireland from 25 October 1760 until 1 January 1801, and there after King of the United Kingdom of Great Britain and Ireland until his death. ...

To a small extent, hemoglobin A slowly combines with glucose at a certain location in the molecule. The resulting molecule is often referred to as Hb A_1c. As the concentration of glucose in the blood increases, the percentage of Hb A that turns into Hb A_1c increases. In diabetics whose glucose usually runs high, the percent Hb A_1c also runs high. Because of the slow rate of Hb A combination with glucose, the Hb A_1c percentage is representative of glucose level in the blood averaged over a longer time (the half-life of red blood cells, which is typically 50-55 days). Glucose (Glc), a monosaccharide, is one of the most important carbohydrates. ... HbA1c is shorthand for glycated hemoglobin A1c, a surrogate marker for blood glucose levels. ... In chemistry, concentration is the measure of how much of a given substance there is mixed with another substance. ... For the disease characterised by excretion of large amounts of severely diluted urine, see diabetes insipidus. ...

Diagnostic use

Hemoglobin levels are amongst the most commonly performed blood tests, usually as part of a full blood count or complete blood count. Results are reported in g/L, g/dL or mol/L. For conversion, 1 g/dl is 0.62 mmol/L. If the hemoglobin level falls below a set point this is called anemia. Anemias are classified by the size of the red blood cells, which are the cells which contain hemoglobin. They can be classified as microcytic (small sized red blood cells), normocytic (normal sized red blood cells) and macrocytic (large sized red blood cells). Blood tests are laboratory tests done on blood to gain an appreciation of disease states and the function of organs. ... A full blood count (FBC) or complete blood count (CBC) is a test requested by a doctor or other medical professional that gives information about the cells in a patients blood. ... A complete blood count (CBC) or full blood count (FBC) is a test requested by a doctor or other medical professional that gives information about the cells in a patients blood. ... The gram or gramme, symbol g, is a unit of mass. ... The litre (or liter in US) is a metric unit of volume. ... The gram or gramme, symbol g, is a unit of mass. ... A decilitre (or deciliter), abbreviated dL or dl, is one tenth of a litre, or 1×10−4 m3, or 100 millilitre. ... The mole and its simple conversions into different units of measurements. ... This article discusses the medical condition. ...

Glucose levels in blood can vary widely each hour, so one or only a few samples from a patient analyzed for glucose may not be representative of glucose control in the long run. For this reason a blood sample may be analyzed for Hb A_1c level, which is more representative of glucose control averaged over a longer time period (determined by the half-life of the individual's red blood cells, which is typically 50-55 days). People whose Hb A_1c runs 6.0% or less show good longer-term glucose control. Hb A_1c values which are more than 7.0% are elevated. This test is especially useful for diabetics. In medicine, blood sugar is a term used to refer to levels of glucose in the blood. ... For the disease characterised by excretion of large amounts of severely diluted urine, see diabetes insipidus. ...

This Hb A_1c level is only useful in individuals who have red blood cells (RBCs) with normal survivals (i.e., normal half-life). In individuals with abnormal RBCs, whether due to abnormal hemoglobin molecules (such as Hemoglobin S in Sickle Cell Anemia) or RBC membrane defects - or other problems, the RBC half-life is frequently shortened. In these individuals an alternative test called "fructosamine level" can be used. It measures the degree of glycation (glucose binding) to albumin, the most common blood protein, and reflects average blood glucose levels over the previous 18-21 days, which is the half-life of albumin molecules in the circulation.

Other biological oxygen-binding proteins

Hemoglobin is by no means unique; there are a variety of oxygen transport and binding proteins throughout the animal (and plant) kingdom. Other organisms including bacteria, protozoans and fungi all have hemoglobin-like proteins whose known and predicted roles include the reversible binding of gaseous ligands. Subgroups Actinobacteria Aquificae Bacteroidetes/Chlorobi Chlamydiae/Verrucomicrobia Chloroflexi Chrysiogenetes Cyanobacteria Deferribacteres Deinococcus-Thermus Dictyoglomi Fibrobacteres/Acidobacteria Firmicutes Fusobacteria Gemmatimonadetes Nitrospirae Planctomycetes Proteobacteria Spirochaetes Thermodesulfobacteria Thermomicrobia Thermotogae Bacteria (singular: bacterium) are a major group of living organisms. ... Protozoa (in Greek proto = first and zoa = life) are single-celled eukaryotes (organisms with nuclei) that show some characteristics usually associated with animals, most notably mobility and heterotrophy. ... Divisions Chytridiomycota Zygomycota Ascomycota Basidiomycota The Fungi (singular: fungus) are a large group of organisms ranked as a kingdom within the Domain Eukaryota. ... It has been suggested that this article or section be merged with Ligand (biochemistry). ...

Myoglobin: Found in the muscle tissue of many vertebrates including humans (gives muscle tissue a distinct red or dark gray color). Is very similar to hemoglobin in structure and sequence, but is not arranged in tetramers, it is a monomer and lacks cooperative binding and is used to store oxygen rather than transport it. Myoglobin is a single-chain protein of 153 amino acids, containing a heme (iron-containing porphyrin) group in the center. ... In biochemistry, a macromolecule has cooperative binding if when binding a ligand, the affinity of the ligand for the molecule changes depending on the amount of ligand already bound. ...

Hemocyanin: Second most common oxygen transporting protein found in nature. Found in the blood of many arthropods and molluscs. Uses copper prosthetic group instead of iron heme groups and is blue in color when oxygenated. Single Oxygenated Hemocyanin protein from Octopus Hemocyanins (also spelled haemocyanins) are respiratory proteins containing two copper atoms that reversibly bind a single oxygen molecule (O2). ... Subphyla and Classes Subphylum Trilobitomorpha Trilobita - trilobites (extinct) Subphylum Chelicerata Arachnida - spiders, scorpions, etc. ... Classes Caudofoveata Aplacophora Polyplacophora - Chitons Monoplacophora Bivalvia - Bivalves Scaphopoda - Tusk shells Gastropoda - Snails and Slugs Cephalopoda - Squids, Octopuses, etc. ...

Hemerythrin: Some marine invertebrates and a few species of annelid use this iron containing non-heme protein to carry oxygen in their blood. Appears pink/violet when oxygenated, clear when not. Single Oxygenated Hemerythrin protein Trimeric Hemerythrin Protein Complex Hemerythrin (also spelled haemerythrin; from Greek words αίμα = blood and ερυθρός = red) is an oligomeric protein responsible for oxygen (O2) transportation in the marine invertebrate phyla of sipuniculids, priapulids, brachiopods, and in a single annelid worm, magelona. ... Classes and subclasses Class Polychaeta      (paraphyletic?) Class Clitellata    Oligochaeta-      (Earthworms, etc. ...

Chlorocruorin: Found in many annelids, and is very similar to Erythrocruorin, but the heme group is significantly different in structure. Appears green when deoxygenated and red when oxygenated. Chlorocruorin is the chemical substance supposed to cause the green color of the blood of certain worms. ... Classes and subclasses Class Polychaeta      (paraphyletic?) Class Clitellata    Oligochaeta-      (Earthworms, etc. ...

Vanabins: Also known as Vanadium Chromagen are found in the blood of Sea squirt and are hypothesised to use the rare metal Vanadium as its oxygen binding prosthetic group, but this hypothesis is unconfirmed. Vanabins (also known as vanadium-associated proteins or vanadium chromagen) are a class of metalloproteins containing vanadium. ... Vanadium is a chemical element in the periodic table that has the symbol V and atomic number 23. ... Classes Ascidiacea Thaliacea Appendicularia Urochordata (sometimes known as tunicata and commonly called urochordates, tunicates or sea squirts) is the subphylum of saclike filter feeders with input and output siphons. ...

Erythrocruorin: Found in many annelids, including earthworms. Giant free-floating blood protein, contains many dozens even hundreds of Iron heme containing protein subunits bound together into a single protein complex with a molecular masses greater than 3.5 million daltons. Classes and subclasses Class Polychaeta      (paraphyletic?) Class Clitellata    Oligochaeta-      (Earthworms, etc. ... Families Suborder Haplotaxina   Haplotaxidae Suborder Moniligastrina   Moniligastridae Suborder Lumbricina   Alluroididae   Eudrilidae   Glossoscolecidae   Lumbricidae   Sparganophilidae   Acanthodrilidae   Octochaetidae   Exxidae   Megascolecidae   Microchaetidae   Eudrilidae Suborder Tubificina   Dorydrilidae   Enchytraeidae   Naididae   Opistocystidae   Phreodrilidae   Tubificidae Earthworm is the common name for the larger members of the Oligochaeta (which is either a class or subclass depending on the...

Pinnaglobin: Only seen in the mollusk Pinna squamosa. Brown manganese-based porphyrin protein. Classes Caudofoveata Aplacophora Polyplacophora Monoplacophora Bivalvia Scaphopoda Gastropoda Cephalopoda † Rostroconchia The molluscs or mollusks are the large and diverse phylum Mollusca, which includes a variety of familiar creatures well-known for their decorative shells or as seafood. ...

Leghemoglobin: In leguminous plants, such as alfalfa or soybeans, the nitrogen fixing bacteria in the roots are protected from oxygen by this iron heme containing, oxygen binding protein. The oxygen carrier leghemoglobin (also legoglobin) is a hemoprotein found in leguminous plants. ...

See also

• Haemoprotein
• Haemocyanin
• Chlorophyll
• Haemoglobin A1C
• Haemoglobin S
• Haemoglobin C
• Haemoglobin F
• Haemoglobin A2

Single Oxygenated Hemocyanin protein from Octopus Hemocyanins (also spelled haemocyanins) are respiratory proteins containing two copper atoms that reversibly bind a single oxygen molecule (O2). ... Chlorophyll is a green photosynthetic pigment found in plants, algae, and cyanobacteria. ... HbA1c is shorthand for glycated hemoglobin A1c, a surrogate marker for blood glucose levels. ... Sickle-shaped red blood cells Sickle cell disease is a general term for a group of genetic disorders caused by sickle hemoglobin (Hgb S). ... Fetal hemoglobin protein structure Fetal hemoglobin (also hemoglobin F or HbF) is the main oxygen transport protein in the fetus during the last seven months of development in the womb. ...

References

• Campbell, Mary K. (1999), Biochemistry (Third Edition), Harcourt College Publishers, ISBN 0-03024-426-9.
• Reece, JB (2005), Biology (Seventh Edition), Benjamin Cummings, ISBN 0-8053-7171-0.
• Di Maio, M, Pisano, C & Tambaro, R, Greggi S, Casella G, Laurelli G, Formato R, Iaffaioli RV, Perrone F & Pignata S (2006), "The prognostic role of pre-chemotherapy hemoglobin level in patients with ovarian cancer", Front Biosci, vol. 11:1585-90. PMID 16368539.
• Eshaghian, S, Horwich, TB & Fonarow, GC (2006), "An unexpected inverse relationship between HbA1c levels and mortality in patients with diabetes and advanced systolic heart failure", Am Heart J, vol. 151(1):91. PMID 16368297.
• Hardison, RC (1996), "A brief history of hemoglobins: plant, animal, protist, and bacteria", Proc Natl Acad Sci USA. PMID 8650150.
• Kneipp, J, Balakrishnan, G & Chen, R, Shen TJ, Sahu SC, Ho NT, Giovannelli JL, Simplaceanu V, Ho C, Spiro TG (2005), "Dynamics of Allostery in Hemoglobin: Roles of the Penultimate Tyrosine H bonds", J Mol Biol. PMID 16368110.
• Ganong, William F. (2003), Review of Medical Physiology (Twenty-First Edition), Lange Medical Books (McGraw-Hill Medical Publishing Division), ISBN 0-07140-236-5.

External links

• Interactive models of hemoglobin (Requires MDL Chime)