No abstract

Porphyrins can be widely used as active-site biocomplexes, where biomimetic synthetic metal porphyrin is considered as being pseudo-enzyme. The system consisted of porphyrinmetal-cysteine (Cys) complex and PEG polymer or mixed SDS/ DTAB surfactants has used to model native chloroperoxidase (CLP). Metal-tetra(2-pyridyl)porphyrins (M-TPP) as more potent than heme (native active-site) were designed and synthesized based on lowering Michaeilis-Menten parameter. Fe-TTP has the maximum CLP activity among central metal including iron (+ 3), manganese(+ 3) and zinc(+ 2). Triple-component: Fe-TPP/ Cys/PEG, indicated most efficient "nanozyme" toward native CLP efficiency. It can be seen that porphyrin hydrophobicity varies by changing central metal, detected via Thioflavin T fluorescence method such as Fe(+ 3) > Mn(+ 3) > Zn(+ 2) attributed to charge transfer between π-electron and central metal. Dynamic light scattering indicates that the addition of Fe-TPP/Cys, as PEG absorbent nucleus, causes nano-particle creation. Transmission electron microscopy illustrated multiholes vesicular Fe-TPP/Cys/PEG nanozyme that causes more efficiency via higher specific surface area for substrate trap comparing one-hole vesicular Fe-TPP/Cys/SDS/DTAB biocatalyst. Presence of Fe-TPP/Cys active-site inside nanozyme was confirmed by UV-Visible spectroscopy as well as Circular dichroism. Differential scanning calorimetry indicates more single colloid structure for PEG nanozyme than attributed SDS/ DTAB biocatalyst.