Examples of hemoglobin in the following topics:
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- Carbon monoxide molecules compete with oxygen to bind to hemoglobin; as a result, not enough oxygen can bind to the hemoglobin.
- Furthermore, carbon monoxide molecules will not detach from hemoglobin, leaving them bound to the protein for long periods of time.
- When oxygen can no longer circulate in the bloodstream (because most or all of the body's hemoglobin are bound to carbon monoxide), nausea and faintness result, followed by organ failure and potentially death.
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- The examples of mellitin, collagen and hemoglobin, shown below demonstrate this feature.
- The hemoglobin molecule is an assembly of four protein subunits, two alpha units and two beta units.
- A model of hemoglobin was shown above, and may also be examined in the image below:
- Hemoglobin's oxygen-binding capacity is decreased in the presence of carbon monoxide because both gases compete for the same binding sites on hemoglobin.
- The binding affinity of hemoglobin for CO is 200 times greater than its affinity for oxygen.
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- Perhaps most famous are the tetradentate N4 macrocyclic ligands incorporated into the heme protein (most commonly seen as part of hemoglobin).
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- Such chelating agents include the porphyrin rings in hemoglobin and chlorophyll.
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- Increased O2 concentration in the lungs helps to displace carbon monoxide from the heme group of hemoglobin.
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- Hydrogen sulfide gas and the hydrosulfide anion are extremely toxic to mammals, because they inhibit the oxygen-carrying capacity of hemoglobin and certain cytochromes in a manner similar to cyanide and azide.
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- Iron plays an important role in biology, forming complexes with molecular oxygen in hemoglobin and myoglobin.
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- In the form of hemoglobin, myoglobin and various lipoproteins, they effect the transport of oxygen and other substances within an organism.
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