The characteristics of binding reaction between bovine serum albumin (BSA) and zincon (ZCN) were studied by fluorescence spectra and ultraviolet-visible absorption spectra. The bovine serum albumin can emit fluorescence (lamda(em) = 345 nm) under irradiation of ultraviolet light (lamda(ex) = 280 nm). After the zincon (ZCN) was added into BSA solution the fluorescence of BSA was quenched partially. The results indicated that ZCN was strongly bound to BSA. According to Stern-Volmer equation and Lineweaver-Burk equation, the quenching constant and the thermodynamic parameters were obtained. From the thermodynamic parameters the binding power between ZCN and BSA can be judged. The binding distance (r = 5.07 nm) and energy transfer efficiency (E = 0.67) between donor (BSA) and acceptor (ZCN) were obtained by Forster's non-radiative energy transfer mechanism. It is confirmed that the combination reaction between ZCN and BSA is a single static quenching process, and their interaction may be interpreted with energy transfer mechanism.