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Facilitated diffusion is the process of spontaneous passive transport of molecules or ions across a biological membrane via specific transmembrane integral proteins. Being passive, facilitated transport does not directly require chemical energy from ATP hydrolysis in the transport step itself; rather, molecules and ions move down their concentration gradient reflecting its diffusive nature.
Hemoglobin or haemoglobin, abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the lungs or gills to the rest of the body. There it releases the oxygen to permit aerobic respiration to provide energy to power the functions of the organism in the process called metabolism. A healthy individual has 12 to 20 grams of hemoglobin in every 100 mL of blood.
Iron is a chemical element with symbol Fe and atomic number 26. It is a metal that belongs to the first transition series and group 8 of the periodic table. It is, by mass, the most common element on Earth, right in front of oxygen, forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust.
Myoglobin is an iron- and oxygen-binding protein found in the cardiac and skeletal muscle tissue of vertebrates in general and in almost all mammals. Myoglobin is distantly related to hemoglobin. Compared to hemoglobin, myoglobin has a higher affinity for oxygen and does not have cooperative binding with oxygen like hemoglobin does. In humans, myoglobin is only found in the bloodstream after muscle injury.
A hemeprotein, or heme protein, is a protein that contains a heme prosthetic group. They are a very large class of metalloproteins. The heme group confers functionality, which can include oxygen carrying, oxygen reduction, electron transfer, and other processes. Heme is bound to the protein either covalently or noncovalently or both.
Leghemoglobin is an oxygen-carrying phytoglobin found in the nitrogen-fixing root nodules of leguminous plants. It is produced by these plants in response to the roots being colonized by nitrogen-fixing bacteria, termed rhizobia, as part of the symbiotic interaction between plant and bacterium: roots not colonized by Rhizobium do not synthesise leghemoglobin. Leghemoglobin has close chemical and structural similarities to hemoglobin, and, like hemoglobin, is red in colour. It was originally thought that the heme prosthetic group for plant leghemoglobin was provided by the bacterial symbiont within symbiotic root nodules. However, subsequent work shows that the plant host strongly expresses heme biosynthesis genes within nodules, and that activation of those genes correlates with leghemoglobin gene expression in developing nodules.
The globins are a superfamily of heme-containing globular proteins, involved in binding and/or transporting oxygen. These proteins all incorporate the globin fold, a series of eight alpha helical segments. Two prominent members include myoglobin and hemoglobin. Both of these proteins reversibly bind oxygen via a heme prosthetic group. They are widely distributed in many organisms.
A period 4 element is one of the chemical elements in the fourth row of the periodic table of the elements. The periodic table is laid out in rows to illustrate recurring (periodic) trends in the chemical behaviour of the elements as their atomic number increases: a new row is begun when chemical behaviour begins to repeat, meaning that elements with similar behaviour fall into the same vertical columns. The fourth period contains 18 elements beginning with potassium and ending with krypton – one element for each of the eighteen groups. It sees the first appearance of d-block in the table.
Metalloprotein is a generic term for a protein that contains a metal ion cofactor. A large proportion of all proteins are part of this category. For instance, at least 1000 human proteins contain zinc-binding protein domains although there may be up to 3000 human zinc metalloproteins.
Sir John Cowdery Kendrew, was an English biochemist, crystallographer, and science administrator. Kendrew shared the 1962 Nobel Prize in Chemistry with Max Perutz, for their work at the Cavendish Laboratory to investigate the structure of heme-containing proteins.
The diving reflex, also known as the diving response and mammalian diving reflex, is a set of physiological responses to immersion that overrides the basic homeostatic reflexes, and is found in all air-breathing vertebrates studied to date. It optimizes respiration by preferentially distributing oxygen stores to the heart and brain, enabling submersion for an extended time.
Carbon monoxide poisoning typically occurs from breathing in carbon monoxide (CO) at excessive levels. Symptoms are often described as "flu-like" and commonly include headache, dizziness, weakness, vomiting, chest pain, and confusion. Large exposures can result in loss of consciousness, arrhythmias, seizures, or death. The classically described "cherry red skin" rarely occurs. Long-term complications may include chronic fatigue, trouble with memory, and movement problems.
The crocodile icefish or white-blooded fish comprise a family (Channichthyidae) of notothenioid fishes found in the Southern Ocean around Antarctica. They are the only known vertebrates to lack hemoglobin in their blood as adults. Icefish populations are known to reside in the Atlantic and Indian sectors of the Southern Ocean, as well as the continental shelf waters surrounding Antarctica. Water temperatures in these regions remain relatively stable, generally ranging from −1.8 to 2 °C. One icefish, Champsocephalus esox, is distributed north of the Antarctic Polar Frontal Zone. At least 16 species of crocodile icefish are currently recognized, although eight additional species have been proposed for the icefish genus Channichthys.
In biochemistry, p50 represents the partial pressure of a gas required to achieve 50% saturation of a particular protein's binding sites. Values of p50 are negatively correlated with substrate affinity; lower values correspond to higher affinity and vice versa. The term is analogous to the Michaelis–Menten constant (KM), which identifies the concentration of substrate required for an enzyme to achieve 50% of its maximum reaction velocity.
Bioinorganic chemistry is a field that examines the role of metals in biology. Bioinorganic chemistry includes the study of both natural phenomena such as the behavior of metalloproteins as well as artificially introduced metals, including those that are non-essential, in medicine and toxicology. Many biological processes such as respiration depend upon molecules that fall within the realm of inorganic chemistry. The discipline also includes the study of inorganic models or mimics that imitate the behaviour of metalloproteins.
A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O2 transport. Other functions performed include O2 storage, CO2 transport, and transportation of substances other than respiratory gases. There are four major classifications of respiratory pigment: hemoglobin, hemocyanin, erythrocruorin–chlorocruorin, and hemerythrin. The heme-containing globin is the most commonly-occurring respiratory pigment, occurring in at least 9 different phyla of animals.
Blood doping is the practice of boosting the number of red blood cells in the bloodstream in order to enhance athletic performance. Because such blood cells carry oxygen from the lungs to the muscles, a higher concentration in the blood can improve an athlete's aerobic capacity (VO2 max) and endurance. Blood doping can be achieved by making the body produce more red blood cells itself using drugs, giving blood transfusions either from another person or back to the same individual, or by using blood substitutes.
2,3-Bisphosphoglyceric acid (2,3-BPG), also known as 2,3-diphosphoglyceric acid (2,3-DPG), is a three-carbon isomer of the glycolytic intermediate 1,3-bisphosphoglyceric acid (1,3-BPG).
Protoporphyrin IX is an organic compound, classified as a porphyrin, that plays an important role in living organisms as a precursor to other critical compounds like heme (hemoglobin) and chlorophyll. It is a deeply colored solid that is not soluble in water. The name is often abbreviated as PPIX.
Dioxygen complexes are coordination compounds that contain O2 as a ligand. The study of these compounds is inspired by oxygen-carrying proteins such as myoglobin, hemoglobin, hemerythrin, and hemocyanin. Several transition metals form complexes with O2, and many of these complexes form reversibly. The binding of O2 is the first step in many important phenomena, such as cellular respiration, corrosion, and industrial chemistry. The first synthetic oxygen complex was demonstrated in 1938 with cobalt(II) complex reversibly bound O2.
References
- Hoffman, B. M.; Petering, D. H (October 1970). "Coboglobins: Oxygen-Carrying Cobalt-Reconstituted Hemoglobin and Myoglobin". Proceedings of the National Academy of Sciences. 67 (2): 637–643. doi: 10.1073/pnas.67.2.637 . PMC 283253 . PMID 4331717.
- Marden, Michael C.; et al. (28 April 2000). "Modulation of the Oxygen Affinity of Cobalt-Porphyrin by Globin". FEBS Letters. 472 (2–3): 221–224. doi:10.1016/S0014-5793(00)01423-X. hdl: 10067/294190151162165141 . PMID 10788615. S2CID 24995840..