TiO2 functionalized by meso-tetrakis (4-carboxyphenyl) porphine was proposed as an enzyme supporter. Laccase molecules were firmly anchored onto the interface of the nanocomplex via the synergy of multiple mutual interactions, including covalent bonding and the adjacent coordination between the enzyme matrix and protein molecules. Morphology, structural features, surface chemistry, and physiochemical properties of the nanocomposite with Laccase tethering were characterized and explored with a variety of techniques such as: microscopy, spectrometry, electrochemistry, etc. The electro-chemical behavior and photoelectrocatalytic function on oxygen reduction reactions were also evaluated. Results from the investigations indicated that interactions between components of the protein carrier and incorporated Laccase molecules would result in partial orderly distribution of Laccase onto the surface of the nanocomplex with an augmentation in the content of hydrophobic α-helix. Such interactions would alter the original mechanism of the electron shuttle in both native Laccase and the Laccase cofactor in that the Laccase T1 site would play the role of inner electron relay. The electro-active site in TiO2 acted as the primary electron acceptor and would dominate the dynamics in charge of transportation. The adjoining ligation between the Lac and porphine derivative would improve the visible irradiation efficiency and catalytic efficacy in the electro-reduction/photo-electrochemical reduction of dissolved O2 to some extent.