The four chemical classes of respiratory pigments are all metalloproteins.
Respiratory pigments bind reversibly with oxygen at specific oxygen-binding sites associated with the metal atoms in their molecular structures.
In hemoglobins, the unit molecule consists of heme bonded with protein.
The heme structure is an iron porphyrin that is identical in all hemoglobin.
Globin varies widely among species and among different molecular forms of hemoglobin within any single species.
Hemoglobins are the most common and widespread respiratory pigments.
Virtually all vertebrates have blood hemoglobin.
The blood-hemoglobin molecules of vertebrates always occur in red blood cells.
Hemocyanins are the second most common of the respiratory pigments, they turn bright blue when oxygenated.
Respiratory pigments increase the oxygen-carrying capacity of blood, meaning the total amount of oxygen that can be carried by each unit of volume.
When respiratory pigments are combined with oxygen, they are considered oxygenated.
When respiratory pigments release oxygen, they are deoxygenated.
The oxygen equilibrium curve of a respiratory pigment shows the relation between the extent of oxygen binding by the pigment and the oxygen partial pressure.
The shape of the oxygen equilibrium curve depends on the degree of cooperativity among oxygen-binding sites on respiratory-pigment molecules.
The Bohr effect is a reduction in oxygen affinity caused by a decrease in pH and/or an increase in CO2 partial pressure.
The Bohr effect typically enhances oxygen delivery because it promotes oxygen unloading in systemic tissues while promoting loading in the breathing organs.
Elevated blood temperatures often decrease the oxygen affinity of respiratory pigments.
Organic molecules and inorganic ions frequently serve as allosteric modulators of respiratory-pigment function.
Respiratory pigments are diverse in their functional properties.
Respiratory pigments can potentially perform oxygen transport, facilitate CO2 transport, transport other substances, blood buffer, and store oxygen.
Blood respiratory pigments typically become well oxygenated in breathing organs, and when animals are at rest, they typically release only a modest fraction of their oxygen to the systemic tissues.
During exercise, oxygen delivery is enhanced by increases in both the extent of pigment unloading and the rate of blood flow.
The oxygen affinities of respiratory pigments are often critical for pigment function.
When oxygen is transferred from one respiratory pigment to another in an individual animal, the pigment receiving the oxygen has a higher oxygen affinity.
Respiratory-pigment physiology undergoes acclimation, as by changes in pigment amounts, synthesis of new molecular forms, or modulation of preexisting forms.
The carbon dioxide equilibrium curve shows the relation between the total carbon dioxide concentration of blood and the CO2 partial pressure.
In water breathers, the CO2 partial pressures of both systemic arterial blood and systemic venous blood are typically low.
In air breathers, blood CO2 partial pressures tend to be far higher and therefore on the flatter portion of the curve.
Most CO2 carried in blood is typically in the form of bicarbonate.
Bicarbonate formation depends on blood buffers and determines the shape of the carbon dioxide equilibrium curve.
Carbonic anhydrase facilitates the uptake and loss of CO2 from the blood.
The neutral pH varies with temperature, being higher at low temperatures than at high ones.
In animals with variable body temperatures, the normal blood pH often varies in parallel with the neutral pH, being displaced in the alkaline direction to a constant extent.
Acidosis and alkalosis are categories of acid-base disturbance.
Within their range of acid-base regulation, animals correct chronic acid-base disturbances by modulating the elimination of CO2, H+, and bicarbonate in regulatory ways.
Blood concentration as a function of oxygen partial pressure.
Oxygen delivery by human blood at rest and during vigorous exercise.
As the oxygen partial pressure of blood falls, less and less of a drop in partial pressure is required to cause unloading of 5 ml of oxygen from each 100 ml of blood.
The partial pressure of oxygen at which a pigment is 50% saturated shifts.
The Bohr effect: affinity for oxygen decreases as pH decreases or CO2 partial pressure increases.