what does haemoglobin contain?

Answer 1

Haemoglobin is a protein and all proteins contain the elements Nitrogen, Hydrogen, Carbon and Oxygen only but Haemoglobin also contains Iron. =]

Answer 2

Hemoglobin (American English) or haemoglobin (British English) is the iron-containing oxygen-transport metalloprotein in the red blood cells of the blood in vertebrates and other animals. In mammals the protein makes up about 97% of the red cell’s dry content, and around 35% of the total content (including water). Hemoglobin transports oxygen from the lungs or gills to the rest of the body, such as to the muscles, where it releases the oxygen load. Hemoglobin also has a variety of other gas-transport and effect-modulation duties, which vary from species to species, and may be quite diverse in invertebrates.

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 type of hemoglobin in mammals contains four such subunits, each with one heme group.

See more at: http://en.wikipedia.org/wiki/Haemoglobin

Answer 3

haemoglobin is the iron-containing oxygen-transport metalloprotein in the red blood cells of the blood in vertebrates and other animals.

In humans, 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. Each protein chain arranges into a set of alpha-helix structural segments connected together in a globin fold arrangement, so called because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin. This folding pattern contains a pocket which strongly binds the heme group.

Answer 4

Haemoglobin is a globular protein divided into four subunits. Each one of these subunits contains iron IONS. It is these ions which enable the haemoglobin to transport oxygen around the cardiovascular system. The oxygen will not bind to iron atoms, only iron ions because of their charge and the way molecules bind together (polarity, electrostatics etc bla bla bla...)

Other than that, as has been said many many MANY times before, it is proteins made up of lots of little amino acids.

Answer 5

Hemoglobin or haemoglobin is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals. The molecule consists of globin, the apoprotein, and four haem groups, an organic molecule with an iron atom.

Answer 6

Hb is quite a large protein, made of 4 subunits (2 alpha and 2 beta). Each of them is made of aminoacids, just like any protein.
At the point where the 4 units contact each other, there is a complex chemical structure (a pirrolic ring), where there is 1 molecule of iron, that can be bound or not to oxygen. That's how oxygen is transported.

Answer 7

Well like Maureen says its a protein.

But haemoglobin is the protein which carries the oxygen around in your blood. And it makes up our red blood cells.

Answer 8

Structure
Heme groupIn humans, 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. Each protein chain arranges into a set of alpha-helix structural segments connected together in a globin fold arrangement, so called because this arrangement is the same folding motif used in other heme/globin proteins such as myoglobin. This folding pattern contains a pocket which strongly binds the heme group.
A heme group consists of an iron (Fe) atom held in a heterocyclic ring, known as a porphyrin. The iron atom, which is the site of oxygen binding, bonds with the four nitrogens in the center of the ring, which all lie in one plane. The iron is also bound strongly to the globular protein via the imidazole ring of a histidine residue below the porphyrin ring. A sixth position can reversibly bind oxygen, completing the octahedral group of six ligands. Oxygen binds in an "end-on bent" geometry where one oxygen atom binds Fe and the other protrudes at an angle. When oxygen is not bound, a very weakly bonded water molecule fills the site, forming a distorted octahedron.
The iron atom may either be in the Fe2+ or Fe3+ state, but ferrihemoglobin (methemoglobin) (Fe3+) cannot bind oxygen. In binding, oxygen temporarily oxidizes Fe to (Fe3+), so iron must exist in the +2 oxidation state in order to bind oxygen. The body reactivates hemoglobin found in the inactive (Fe3+) state by reducing the iron center.
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, each made of 141 and 146 amino acid residues, respectively. This is denoted as α2β2. The subunits are structurally similar and about the same size. Each subunit has a molecular weight of about 17,000 daltons, for a total molecular weight of the tetramer of about 68,000 daltons. Hemoglobin A is the most intensively studied of the hemoglobin molecules.
The four polypeptide chains are bound to each other by salt bridges, hydrogen bonds, and hydrophobic interactions. There are two kinds of contacts between the α and β chains: α1β1 and α1β2.
Oxyhemoglobin is formed during respiration when oxygen binds to the heme component of the protein hemoglobin in red blood cells. This process occurs in the pulmonary capillaries adjacent to the alveoli of the lungs. The oxygen then travels through the blood stream to be dropped off at cells where it is utilized in aerobic glycolysis and in the production of ATP by the process of oxidative phosphorylation. It doesn't however help to counteract a decrease in blood pH. Ventilation, or breathing, may reverse this condition by removal of carbon dioxide, thus causing a shift up in pH.
Deoxyhemoglobin is the form of hemoglobin without the bound oxygen. The absorption spectra of oxyhemoglobin and deoxyhemoglobin differ. The oxyhemoglobin has significantly lower absorption of the 660 nm wavelength than deoxyhemoglobin, while at 940 nm its absorption is slightly higher. This difference is used for measurement of the amount of oxygen in patient's blood by an instrument called pulse oximeter

Answer 9

Hemoglobin Contains Which Element

Answer 10

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 .and also contains oxygen..





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