The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.
The 18-electron cycle of porphin, the parent structure of porphyrin, highlighted. (Several other choices of atoms, through the pyrrole nitrogens, for example, also give 18-electron cycles.)
A simple [Fe2S2] cluster containing two iron atoms and two sulfur atoms, coordinated by four protein cysteine residues.
Porphycene, first porphyrin isomer, synthesised from bipyrrole dialdehyde through McMurry coupling reaction
The redox reactions of nicotinamide adenine dinucleotide.
Various reported Isomers of porphyrin
Heme B biosynthesis pathway and its modulators. Major enzyme deficiences are also shown.
Brilliant crystals of meso-tetratolylporphyrin, prepared from 4-methylbenzaldehyde and pyrrole in refluxing propionic acid
On a gold surface porphyrin derivative molecules (a) form chains and clusters (b). Each cluster in (c,d) contains 4 or 5 molecules in the core and 8 or 10 molecules in the outer shells (STM images).
An example of porphyrins involved in host–guest chemistry. Here, a four-porphyrin–zinc complex hosts a porphyrin guest.
Porphin is the simplest porphyrin, a rare compound of theoretical interest.
Derivatives of protoporphyrin IX are common in nature, the precursor to hemes.
Octaethylporphyrin (H{{sub|2}}OEP) is a synthetic analogue of protoporphyrin IX. Unlike the natural porphyrin ligands, OEP{{sup|2−}} is highly symmetrical.
Lewis structure for meso-tetraphenylporphyrin
Simplified view of heme, a complex of a protoporphyrin IX.
UV–vis readout for meso-tetraphenylporphyrin
Light-activated porphyrin. Monatomic oxygen. Cellular aging

One of the best-known families of porphyrin complexes is heme, the pigment in red blood cells, a cofactor of the protein hemoglobin.

- Porphyrin

One diverse set of examples is the heme proteins, which consist of a porphyrin ring coordinated to iron.

- Cofactor (biochemistry)
The succinate dehydrogenase complex showing several cofactors, including flavin, iron–sulfur centers, and heme.

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