Detailed fluorescence studies on bovine heart cytochrome-c oxidase (CcO) has been carried out in lauryl maltoside solution. Steady-state fluorescence of the tryptophan residues of the enzyme showed that the fluorophores are embedded deep inside the hydrophobic protein cavity. Time resolved studies of tryptophan fluorescence of native and heat treated CcO have been carried out in both reduced and oxidised forms using synchronously pumped pulsed picosecond dye laser and single photon counting technique. Decay of the tryptophan fluorescence have been fitted using discrete four exponential model. Amplitude distribution of lifetimes also showed four distinct regions in the analysis of the decay profiles by maximum entropy method (MEM). The results indicate that controlled heat treatment of CcO affects the conformation of the enzyme near the active centers which makes it incapable of active proton pumping while the electron transfer property is still conserved. Reduction of the native CcO is associated with a large conformation change in lauryl maltoside near the active centers which is not observed in case of CcO encapsulated in vesicles. Reduction of the heat treated enzyme was found to have a conformation different from the reduced native CcO.