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|Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)|
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Upon deprotonation, the corrinoid ring is capable of binding cobalt. In vitamin B12, the resulting complex also features a benzimidazole-derived ligand, and the sixth site on the octahedron serves as the catalytic center.
The corrin ring resembles the porphyrin ring, which occurs in hemoglobin. Both feature four pyrrole-like subunits organized into a ring. In contrast to porphyrins, corrins lack one of the carbon groups that link the pyrrole-like units. Thus the large ring has 19 carbons, whereas porphyrins have 20. Also, the pyrrole-like rings in corrin are fully saturated "edge-carbon" centers. Because of the high number of sp3 carbon centers, corrins are more flexible than porphyrins and are not as flat. They do not have a full conjugated character around the entire ring. Instead, the ring has a kind of "3/4" conjugation.
- Nelson, D. L.; Cox, M. M. "Lehninger, Principles of Biochemistry" 3rd Ed. Worth Publishing: New York, 2000. ISBN 1-57259-153-6.