Porphyrin assemblies and their scaffolds.

The chlorophyll and heme molecules of chloroplasts and mitochondria are brought to life by "the global fold of the protein scaffolds". Proteins in hydrophobic cell regions touch the dye platelets from both sides, pushing and orienting them according to their life-spending activities in light and electron transfers. The conjugated π-electron systems or planarity of the porphyrin macrocycles are never disturbed. Most artificial porphyrin assemblies contain meso-tetraphenylporphyrins (TPPs), because the four phenyl groups rotate freely and carry their substituents above or below the macrocycle. A single porphyrin molecule can, for example, be attached to an anionic surface with ammonium groups on its 2,3-carbons, be located within a hydrophobic membrane with its alkyl chains on the 4-position, and then fixate a cationic polymer with 4,5-sulphonates. Charged TPPs also show unique spectroscopic changes at different pH values and a reversible loss of the macrocycle's planarity. On smooth silicate, graphite, or gold scaffolds TPPs have been attached irreversibly as single molecules, as extended non-covalent H or J aggregates as well as acetylene or thiophene-linked polymers. Soft, mobile porphyrin ladders conduct excited electrons ("excitons") better than rigid porphyrin wires ("polarons").