Biologic and synthetic porphyrins have been used in many studies that involve clinical biochemistry, photodynamic therapy, biocatalysis, supramolecular chemistry, nanotechnology and other areas. Porphyrins have interesting catalytic properties that can be modulated by their ability to interact with micelles, liposomes, nanoparticles and proteins. The interaction of protoporphyrin IX (the heme group) with apoproteins is widespread in nature and produces holoproteins responsible for vital process such as cell respiration, metabolism of xenobiotics, oxygen transport and combat to free radicals. The association of porphyrins with proteins can involve coordination with the metal center and hydrophobic interactions and, in the case of cytochromes c and mammalian peroxidases, the formation of covalent bonds. In this work, we describe the incorporation to FeTDC(SO₃Na)PP, a synthetic, non-biological porphyrin, by apocytochrome c and myoglobin. The UV-visible spectroscopy analysis of the porphyrin revealed that the association with cytochrome c and apomyoglobin led to Soret band blue shift from 412 to 420 nm compatible with the placement of the prosthetic group in a hydrophobic microenvironment and maybe in the hexacoordinated form. The formation of the non-covalent complex of FeTDC(SO₃Na)PP with apohemoproteins led also to an increase in the sample turbidity suggesting the formation of a quaternary structure with a high number of subunits. The catalytic activity of these complexes was compared with that observed when the porphyrin was in homogeneous media or associated to CTAB or SDS micelles. In the absence of apoproteins, FeTDC(SO₃Na)PP was reduced by diphenylacetaldehyde (DPAA) but exhibited only a discrete bleaching when incubated with the aldehyde in the non-covalent complex forms. In the absence of apoproteins, the reaction with t-butyl-hydroperoxide promoted a peroxidase-like catalytic cycle but the formation of the high valent peroxidases intermediates were not observed when FeTDC(SO₃Na)PP was associated to apoproteins and the Soret band bleaching was also observed. The occurrence of Soret band bleaching indicates the formation of free radicals due to the porphyrin-promoted reagents cleavage and the exact catalytic mechanism exhibited by these non-covalent complexes is our investigation scope herein.