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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. [2] [3] 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 porphyrin with a core phosphorus (V) ion can be tuned with additional substituents added to either the outside of the polycyclic ring system or axially to the core phosphorus. Meso-substituted porphyrins like meso-tetra-p-tolylporphyrin (TTP) and octaethylporphyrin (OEP) are often used in synthesis of the core phosphorus porphyrin.
In the typical porphyrin biosynthesis pathway, four molecules of porphobilinogen are concatenated by carbons 2 and 5 of the pyrrole ring (adjacent to the nitrogen atom) into hydroxymethyl bilane by the enzyme porphobilinogen deaminase, also known as hydroxymethylbilane synthase.
In biochemistry, a porphyrinogen is a member of a class of naturally occurring compounds with a tetrapyrrole core, a macrocycle of four pyrrole rings connected by four methylene bridges. [1] They can be viewed as derived from the parent compound hexahydroporphine by the substitution of various functional groups for hydrogen atoms in the ...
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. [3]
The porphyrin ring is a planar dianionic, tetradentate ligand. The iron is typically Fe 2+ or Fe 3+. One or two ligands are attached at the axial sites. The porphyrin ring has 4 nitrogen atoms that bind to the iron, leaving two other coordination positions of the iron available for bonding to the histidine of the protein and a divalent atom. [2]
Four pyrrole rings are joined in a ring structure called a porphyrin. The rings of porphyrin are components of hemoglobin , myoglobin , vitamin B12 , chlorophyll , and cytochromes . In the centers of heme in hemoglobin, myoglobin, and cytochromes, iron is an ion; in the first two, iron ion is bound to oxygen.
The heme group uses four equatorial ligands in the porphyrin ring, with the two axial ligands being the histidine side chain and molecular oxygen. Heme proteins are proteins that contain a heme prosthetic group. The heme group consists of a porphyrin ring coordinated with an iron ion. Four nitrogen atoms in the porphyrin ring act as a ligand ...