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Methemoglobin cannot bind oxygen, which means it cannot carry oxygen to tissues. It is bluish chocolate-brown in color. It is bluish chocolate-brown in color. In human blood a trace amount of methemoglobin is normally produced spontaneously, but when present in excess the blood becomes abnormally dark bluish brown.
The binding of oxygen to methemoglobin results in an increased affinity for oxygen in the remaining heme sites that are in ferrous state within the same tetrameric hemoglobin unit. [17] This leads to an overall reduced ability of the red blood cell to release oxygen to tissues, with the associated oxygen–hemoglobin dissociation curve ...
Nevertheless, if the binding capacities of haptoglobin and hemopexin are saturated [note 1], the remaining "free hemoglobin" in the plasma will be oxidized to met-hemoglobin eventually, and then further disassociates into free heme and others. [3] At this stage, the "free heme" will bind to albumin, forming met-hemalbumin.
Hemoglobin has an oxygen binding capacity between 1.36 and 1.40 ml O 2 per gram hemoglobin, [23] which increases the total blood oxygen capacity seventyfold, [24] compared to if oxygen solely were carried by its solubility of 0.03 ml O 2 per liter blood per mm Hg partial pressure of oxygen (about 100 mm Hg in arteries).
Initial oxidation to the ferric (Fe 3+) state without oxygen converts hemoglobin into "hemiglobin" or methemoglobin, which cannot bind oxygen. Hemoglobin in normal red blood cells is protected by a reduction system to keep this from happening. Nitric oxide is capable of converting a small fraction of hemoglobin to methemoglobin in red blood cells.
This causes a leftward shift in the oxygen hemoglobin dissociation curve, as any residual heme with oxygenated ferrous iron (+2 state) is unable to unload its bound oxygen into tissues (because 3+ iron impairs hemoglobin's cooperativity), thereby increasing its affinity with oxygen. However, methemoglobin has increased affinity for cyanide, and ...
On erythrocytes, red blood cells, the c5br enzyme is responsible for the recycling and conversion of methemoglobin to hemoglobin. [6] Methemoglobin is an oxidized form of hemoglobin attached to a ferric-state iron (Fe3+), which can therefore not carry and deliver oxygen to tissues. [15]
Blood viscosity is a measure of the resistance of blood to flow. It can also be described as the thickness and stickiness of blood. This biophysical property makes it a critical determinant of friction against the vessel walls, the rate of venous return, the work required for the heart to pump blood, and how much oxygen is transported to tissues and organs.