Hemoglobin

haemoglobinoxyhemoglobindeoxyhemoglobinoxyhaemoglobinadult hemoglobinhemoglobinsdeoxyhaemoglobinh'''a'''emoglobinHemooxygen-binding
Hemoglobin (American English) or haemoglobin (British English), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae ) as well as the tissues of some invertebrates.wikipedia
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Metalloprotein

metalloenzymemetalloenzymesmetalloproteins
Hemoglobin (American English) or haemoglobin (British English), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae ) as well as the tissues of some invertebrates.
For instance, the relatively high concentration of iron in the human body is mostly due to the iron in hemoglobin.

Iron

FeFe 2+ Fe(III)
Hemoglobin (American English) or haemoglobin (British English), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae ) as well as the tissues of some invertebrates.
The body of an adult human contains about 4 grams (0.005% body weight) of iron, mostly in hemoglobin and myoglobin.

Channichthyidae

crocodile icefishIcefishchannichthyid
Hemoglobin (American English) or haemoglobin (British English), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae ) as well as the tissues of some invertebrates.
They are the only known vertebrates to lack hemoglobin in their blood as adults.

Anemia

anaemiaanemicanaemic
This is an effect of intravascular hemolysis, in which hemoglobin separates from red blood cells, a form of anemia.
Anemia (also spelled anaemia) is a decrease in the total amount of red blood cells (RBCs) or hemoglobin in the blood, or a lowered ability of the blood to carry oxygen.

Hemoglobinemia

hemoglobin directly into the blood vessels
Hemoglobinemia is a medical condition in which there is an excess of hemoglobin in the blood plasma.
Hemoglobinemia (British Haemoglobinaemia) is a medical condition in which there is an excess of hemoglobin in the blood plasma.

Red blood cell

red blood cellserythrocyteserythroid
Hemoglobin (American English) or haemoglobin (British English), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae ) as well as the tissues of some invertebrates. This is an effect of intravascular hemolysis, in which hemoglobin separates from red blood cells, a form of anemia.
The cytoplasm of erythrocytes is rich in hemoglobin, an iron-containing biomolecule that can bind oxygen and is responsible for the red color of the cells and the blood.

Max Perutz

Max Ferdinand PerutzMax F. PerutzDr Max Perutz
In 1959, Max Perutz determined the molecular structure of hemoglobin by X-ray crystallography.
Max Ferdinand Perutz (19 May 1914 – 6 February 2002) was an Austrian-born British molecular biologist, who shared the 1962 Nobel Prize for Chemistry with John Kendrew, for their studies of the structures of haemoglobin and myoglobin.

Carbaminohemoglobin

carbaminohaemoglobin
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 2 is bound to the heme protein.
Carbaminohaemoglobin (or carbaminohaemoglobin, also known as carbhaemoglobin and carbohaemoglobin) is a compound of hemoglobin and carbon dioxide, and is one of the forms in which carbon dioxide exists in the blood.

Heme

haemheme grouphaeme
The name hemoglobin is derived from the words heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group.
Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochromes, catalases, heme peroxidase, and endothelial nitric oxide synthase.

Hemoglobin A

HbAadult hemoglobinadult
There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present) is coded for by the genes, HBA1, HBA2, and HBB.
Hemoglobin A (HbA), also known as adult hemoglobin, hemoglobin A1 or α 2 β 2, is the most common human hemoglobin tetramer, accounting for over 97% of the total red blood cell hemoglobin.

Hemoglobin variants

hemoglobin variantvariant
Mutations in the genes for the hemoglobin protein in a species result in hemoglobin variants.
Hemoglobin variants are mutant forms of hemoglobin in a population (usually of humans), caused by variations in genetics.

Thalassemia

thalassaemiathalassaemiasBeta-Thalassemia
A (mostly) separate set of diseases called thalassemias involves underproduction of normal and sometimes abnormal hemoglobins, through problems and mutations in globin gene regulation.
Thalassemias are inherited blood disorders characterized by abnormal hemoglobin production.

Hemoglobin, alpha 1

HBA1alpha globinalpha
There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present) is coded for by the genes, HBA1, HBA2, and HBB.
Hemoglobin, alpha 1, also known as HBA1, is a hemoglobin protein that in humans is encoded by the HBA1 gene.

HBB

beta-globinbetaBeta globin
There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present) is coded for by the genes, HBA1, HBA2, and HBB.
Beta globin (also referred to as HBB, β-globin, haemoglobin beta, hemoglobin beta, or preferably haemoglobin subunit beta) is a globin protein, which along with alpha globin (HBA), makes up the most common form of haemoglobin in adult humans, the HbA.

Protein subunit

subunitsubunitsprotein subunits
The name hemoglobin is derived from the words heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group.
Some naturally occurring proteins have a relatively small number of subunits and therefore described as oligomeric, for example hemoglobin or DNA polymerase.

Human iron metabolism

iron metabolismironiron homeostasis
In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism.
Heme groups are part of hemoglobin, a protein found in red blood cells that serves to transport oxygen from the lungs to the tissues.

Metabolism

metabolicmetabolizedmetabolic pathways
There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism.
These metals are used in some proteins as cofactors and are essential for the activity of enzymes such as catalase and oxygen-carrier proteins such as hemoglobin.

Leghemoglobin

leghaemoglobinleghaemoglobins
A variant of the molecule, called leghemoglobin, is used to scavenge oxygen away from anaerobic systems, such as the nitrogen-fixing nodules of leguminous plants, lest the oxygen poison (deactivate) the system.
Leghemoglobin has close chemical and structural similarities to hemoglobin, and, like hemoglobin, is red in colour.

Hemoglobin, alpha 2

HBA2alpha-2Alpha globin 2
There is more than one hemoglobin gene: in humans, hemoglobin A (the main form of hemoglobin present) is coded for by the genes, HBA1, HBA2, and HBB.
Hemoglobin, alpha 2 also known as HBA2 is a gene that in humans codes for the alpha globin chain of hemoglobin.

X-ray crystallography

X-ray diffractionprotein crystallographyX-ray
In 1959, Max Perutz determined the molecular structure of hemoglobin by X-ray crystallography.
In 1951, the Festival Pattern Group at the Festival of Britain hosted a collaborative group of textile manufacturers and experienced crystallographers to design lace and prints based on the X-ray crystallography of insulin, china clay, and hemoglobin.

Methemoglobin

methaemoglobinmet-hemoglobinferric hemoglobin
The iron ion may be either in the Fe 2+ or in the Fe 3+ state, but ferrihemoglobin (methemoglobin) (Fe 3+ ) cannot bind oxygen.
Methemoglobin (English: methaemoglobin) (pronounced "met-hemoglobin") is a hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe 3+ (ferric) state, not the Fe 2+ (ferrous) of normal hemoglobin.

Globin

globin foldGlobin superfamilygamma globins
The name hemoglobin is derived from the words heme and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group.
Two prominent members include myoglobin and hemoglobin.

Gilbert Smithson Adair

G.S. Adair
Gilbert Smithson Adair confirmed Engelhard's results in 1925 by measuring the osmotic pressure of hemoglobin solutions.
Gilbert Smithson Adair FRS (1896–1979) was an early protein scientist who used osmotic pressure measurements to establish that haemoglobin was a tetramer under physiological conditions.

Myoglobin

globular proteinsMB
Such a name is given because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin.
It is distantly related to hemoglobin which is the iron- and oxygen-binding protein in blood, specifically in the red blood cells.

Oxygen

OO 2 molecular oxygen
Hemoglobin (American English) or haemoglobin (British English), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae ) as well as the tissues of some invertebrates.
Hemoglobin binds, changing color from bluish red to bright red ( is released from another part of hemoglobin through the Bohr effect).