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THE ROLE OF IRON-PORPHYRIN COMPOUNDS IN BIOLOGICAL OXIDATIONS

1939; Cold Spring Harbor Laboratory Press; Volume: 7; Linguagem: Inglês

10.1101/sqb.1939.007.01.014

1943-4456

E. S. Guzmán Barrón,

Hemoglobin structure and function

The iron-porphyrin compounds occupy a unique position among the oxidation-reduction systems of biological importance, because on combining with nitrogenous compounds they form complexes possessing manifold properties, all of them connected with the function of respiration. Thus, certain iron-prophyrins may combine with a protein and form compounds—hemoglobin, myoglobin, chlorocruorin, erythrocruorin—which have the property of combining reversibly with molecular oxygen with no alteration of the valence number of the Fe atom. Iron-porphyrins may combine with proteins and give non-autoxidizable sluggish oxidation-reduction systems—hemoglobin-methemoglobin, cytochrome-c, cytochrome-a. Finally, they may combine with proteins or other nitrogenous compounds giving autoxidizable, electroactive systems—hemochromogens, cytochromes-b and a3.