In this paper we present a simple method allowing for stable laccase immobilization on various conducting surfaces that retains the activity of the enzyme. The strategy for laccase immobilization presented in this paper relies on Zr(4+) ion coordination chemistry that involves -COO- terminal groups present on the protein. Using a host of techniques, including surface plasmon resonance (SPR), quartz crystal microbalance (QCM) gravimetry, atomic force microscopy (AFM), surface enhanced Raman scattering (SERS), resonance Raman scattering (RR) and electrochemical techniques, we show that laccase bound to a surface coordinatively through zirconium phosphonate/carboxylate (ZPC) functionalities forms a stable enzymatic layer with the enzyme retaining its activity to a significant extent.