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Porphyrins and their metal complexes have been investigated for many years because the richness of the properties of these compounds is of interest to a wide range of scientific disciplines, from medicine to materials science (Figure 1). Metalloporphyrins in living systems play many functions that are essential for life, and the elucidation of both the geometric and electronic structures of these compounds is of extreme relevance to a detailed understanding of their roles in biological systems. Moreover, the possibility of mimicking the complex chemistry exhibited by metalloporphyrins in living organisms with synthetic models propitiates the possibility of exploiting then in a wide range of different applications, from medical diagnostics and treatments to catalysts and sensors (Walker, 2006). The heme groups (iron porphyrins) sites are involved in a range of biological functions. These roles are developed through various biochemical processes, such as electron transfer (e.g., cytochromes a, b, c, and f), in which the heme cycle between low-spin Fe(II) and lowspin Fe(III) small-molecule binding and transport, catalysis, and O2 activation (e.g. peroxidases and cytochromes P450), where high-valent iron centers are involved in several chemical reactions, such as hydrogen atom abstraction, hydroxylation, and epoxide formation (Figure 1). Heme sites are significantly different from non-heme iron sites in which the porphyrin ligand allows the delocalization of the iron d-electrons into the porphyrin π system. This distribution of electronic density changes the properties of the iron with respect to the flexibility of the central coordination site, the energetics of reactivity, and, consequently, to its biological function (Hocking et al., 2007).

Giant Extracellular Hemoglobin of Glossoscolex paulistus: An excellent Prototype of Biosensor and Blood Substitute