The interaction of 2,3-diazabicyclo[2.2.2]oct-2-ene (DBO) with bovine serum albumin (BSA) has been studied using absorption and steady state fluorescence techniques. Fluorescence spectrum of BSA (λ_exi=280nm) in the presence of DBO clearly shows that DBO acts as a quencher. The number of binding sites ‘n’ and apparent binding constant ‘K’ were measured by Stern–Volmer equation. Synchronous fluorescence and absorption spectra were used to study protein conformation. The interaction between DBO and BSA is consistent with static quenching and the conformational changes of BSA observed.