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Protoporphyrin
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. Protoporphyrin IX contains a porphine core, a tetrapyrrole macrocycle with a marked aromatic character. Protoporphyrin IX is essentially planar, except for the N-H bonds that are bent out of the plane of the rings, in opposite (trans) directions. Nomenclature The general term protoporphyrin refers to porphine derivatives that have the outer hydrogen atoms in the four pyrrole rings replaced by other functional groups. The prefix proto often means 'first' in science nomenclature (such as carbon protoxide), hence Hans Fischer is thought to have coined the name protoporphyrin as the first class of porphyrins. Fischer described iron-deprived heme becoming the "proto-" porphyrin, particu ...
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Porphyrin
Porphyrins ( ) are a group of heterocyclic macrocycle organic compounds, composed of four modified pyrrole subunits interconnected at their α carbon atoms via methine bridges (=CH−). The parent of porphyrin is porphine, a rare chemical compound of exclusively theoretical interest. Substituted porphines are called porphyrins. With a total of 26 π-electrons, of which 18 π-electrons form a planar, continuous cycle, the porphyrin ring structure is often described as aromatic. One result of the large conjugated system is that porphyrins typically absorb strongly in the visible region of the electromagnetic spectrum, i.e. they are deeply colored. The name "porphyrin" derives from the Greek word πορφύρα (''porphyra''), meaning ''purple''. Complexes of porphyrins Concomitant with the displacement of two N-''H'' protons, porphyrins bind metal ions in the N4 "pocket". The metal ion usually has a charge of 2+ or 3+. A schematic equation for these syntheses is shown: :H2 ...
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Zinc Protoporphyrin
Zinc protoporphyrin (ZPP) refers to coordination complexes of zinc and protoporphyrin IX. It is a red-purple solid that is soluble in water. The complex and related species are found in red blood cells when heme production is inhibited by lead and/or by lack of iron. Clinical utility Measurement of zinc protoporphyrin in red cells has been used for screening for lead poisoning. and for iron deficiency. Zinc protoporphyrin levels can be elevated as the result of a number of conditions, for instance: *lead poisoning *iron deficiency *sickle cell anemia *sideroblastic anemia *anemia of chronic disease *vanadium exposure *erythropoietic protoporphyria *Diverse types of cancer The virtue of elevated ZPP testing as a ''screen'' is that all of these conditions can be considered worth discovering. The fluorescent properties of ZPP in intact red cells allows the ZPP/heme molar ratio to be measured quickly, at low cost, and in a small sample volume. ZnPP is finding a new use as a drug i ...
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Bilin (biochemistry)
Bilins, bilanes or bile pigments are biological pigments formed in many organisms as a metabolic product of certain porphyrins. Bilin (also called bilichrome) was named as a bile pigment of mammals, but can also be found in lower vertebrates, invertebrates, as well as red algae, green plants and cyanobacteria. Bilins can range in color from red, orange, yellow or brown to blue or green. In chemical terms, bilins are linear arrangements of four pyrrole rings (tetrapyrroles). In human metabolism, bilirubin is a breakdown product of heme. A modified bilane is an intermediate in the biosynthesis and uroporphyrinogen III from porphobilinogen (PBG). Examples of bilins are found in animals (cardinal examples are bilirubin and biliverdin), and phycocyanobilin, the chromophore of the photosynthetic pigment phycocyanin, in algae and plants. In plants, bilins also serve as the photopigments of the photoreceptor protein phytochrome. An example of an invertebrate bilin is micromatabilin, whic ...
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Bilirubin
Bilirubin (BR) (Latin for "red bile") is a red-orange compound that occurs in the normal catabolic pathway that breaks down heme in vertebrates. This catabolism is a necessary process in the body's clearance of waste products that arise from the destruction of aged or abnormal red blood cells. In the first step of bilirubin synthesis, the heme molecule is stripped from the hemoglobin molecule. Heme then passes through various processes of porphyrin catabolism, which varies according to the region of the body in which the breakdown occurs. For example, the molecules excreted in the urine differ from those in the feces. The production of biliverdin from heme is the first major step in the catabolic pathway, after which the enzyme biliverdin reductase performs the second step, producing bilirubin from biliverdin.Boron W, Boulpaep E. Medical Physiology: a cellular and molecular approach, 2005. 984–986. Elsevier Saunders, United States. Ultimately, bilirubin is broken down within ...
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Cytochrome C
The cytochrome complex, or cyt ''c'', is a small hemeprotein found loosely associated with the inner membrane of the mitochondrion. It belongs to the cytochrome c family of proteins and plays a major role in cell apoptosis. Cytochrome c is highly water-soluble, unlike other cytochromes, and is an essential component of the respiratory electron transport chain, where it carries one electron. It is capable of undergoing oxidation and reduction as its iron atom converts between the ferrous and ferric forms, but does not bind oxygen. It transfers electrons between Complexes III (Coenzyme Q – Cyt c reductase) and IV (Cyt c oxidase). In humans, cytochrome c is encoded by the ''CYCS'' gene. Species distribution Cytochrome c is a highly conserved protein across the spectrum of eukaryotic species, found in plants, animals, fungi, and many unicellular organisms. This, along with its small size (molecular weight about 12,000 daltons), makes it useful in studies of clad ...
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Myoglobin
Myoglobin (symbol Mb or MB) 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. (Google books link is the 2008 edition) High concentrations of myoglobin in muscle cells allow organisms to hold their breath for a longer period of time. Diving mammals such as whales and seals have muscles with particularly high abundance of myoglobin. Myoglobin is found in Type I muscle, Type II A, and Type II B; although many texts consider myoglobin not to be found in smooth muscle, this has proved erroneous: there is also myoglobin in smooth muscle cells. Myoglobin was the first protein to have its three-dimensional structure revealed by X-ray crystal ...
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Prosthetic Group
A prosthetic group is the non-amino acid component that is part of the structure of the heteroproteins or conjugated proteins, being tightly linked to the apoprotein. Not to be confused with the cofactor that binds to the enzyme apoenzyme (either a holoprotein or heteroprotein) by non-covalent binding a non-protein (non-amino acid) This is a component of a conjugated protein that is required for the protein's biological activity. The prosthetic group may be organic (such as a vitamin, sugar, RNA, phosphate or lipid) or inorganic (such as a metal ion). Prosthetic groups are bound tightly to proteins and may even be attached through a covalent bond. They often play an important role in enzyme catalysis. A protein without its prosthetic group is called an apoprotein, while a protein combined with its prosthetic group is called a holoprotein. A non-covalently bound prosthetic group cannot generally be removed from the holoprotein without denaturating the protein. Thus, the term ...
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Iron
Iron () is a chemical element with symbol Fe (from la, ferrum) 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 (32.1% and 30.1%, respectively), forming much of Earth's outer and inner core. It is the fourth most common element in the Earth's crust. In its metallic state, iron is rare in the Earth's crust, limited mainly to deposition by meteorites. Iron ores, by contrast, are among the most abundant in the Earth's crust, although extracting usable metal from them requires kilns or furnaces capable of reaching or higher, about higher than that required to smelt copper. Humans started to master that process in Eurasia during the 2nd millennium BCE and the use of iron tools and weapons began to displace copper alloys, in some regions, only around 1200 BCE. That event is considered the transition from the Bronze Age to the ...
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Cation
An ion () is an atom or molecule with a net electrical charge. The charge of an electron is considered to be negative by convention and this charge is equal and opposite to the charge of a proton, which is considered to be positive by convention. The net charge of an ion is not zero because its total number of electrons is unequal to its total number of protons. A cation is a positively charged ion with fewer electrons than protons while an anion is a negatively charged ion with more electrons than protons. Opposite electric charges are pulled towards one another by electrostatic force, so cations and anions attract each other and readily form ionic compounds. Ions consisting of only a single atom are termed atomic or monatomic ions, while two or more atoms form molecular ions or polyatomic ions. In the case of physical ionization in a fluid (gas or liquid), "ion pairs" are created by spontaneous molecule collisions, where each generated pair consists of a free electron ...
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Valence (chemistry)
In chemistry, the valence (US spelling) or valency (British spelling) of an element is the measure of its combining capacity with other atoms when it forms chemical compounds or molecules. Description The combining capacity, or affinity of an atom of a given element is determined by the number of hydrogen atoms that it combines with. In methane, carbon has a valence of 4; in ammonia, nitrogen has a valence of 3; in water, oxygen has a valence of 2; and in hydrogen chloride, chlorine has a valence of 1. Chlorine, as it has a valence of one, can be substituted for hydrogen. Phosphorus has a valence of 5 in phosphorus pentachloride, . Valence diagrams of a compound represent the connectivity of the elements, with lines drawn between two elements, sometimes called bonds, representing a saturated valency for each element. The two tables below show some examples of different compounds, their valence diagrams, and the valences for each element of the compound. Modern definitions ...
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Coordination Compound
A coordination complex consists of a central atom or ion, which is usually metallic and is called the ''coordination centre'', and a surrounding array of bound molecules or ions, that are in turn known as ''ligands'' or complexing agents. Many metal-containing compounds, especially those that include transition metals (elements like titanium that belong to the Periodic Table's d-block), are coordination complexes. Nomenclature and terminology Coordination complexes are so pervasive that their structures and reactions are described in many ways, sometimes confusingly. The atom within a ligand that is bonded to the central metal atom or ion is called the donor atom. In a typical complex, a metal ion is bonded to several donor atoms, which can be the same or different. A polydentate (multiple bonded) ligand is a molecule or ion that bonds to the central atom through several of the ligand's atoms; ligands with 2, 3, 4 or even 6 bonds to the central atom are common. These compl ...
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