Fluorescent probe were used to evaluate the effects of catechin on the structural parameters (annular lipid fluidity, transbilayer lateral and rotational mobility and protein clustering) of the Porphyromonas gingivalis outer membrane (OPGs). An experimental procedure was used on the basis of selective quenching of 1,6-diphenyl-1,3,5-hexatriene (DPH) and 1,3-di(1-pyrenyl)propane (Py-3-Py) by trinitrophenyl groups and radiationless energy transfer from the tryptophans of membrane proteins to Py-3-Py and DPH. Catechin increased the bulk lateral and rotational mobility, annular lipid fluidity of OPGs lipid bilayers, and had greater fluidizing efficacy on the outer monolayer than the inner monolayer. It also caused membrane proteins to cluster. Based on these effects of catechin on OPGs, the antibacterial and antiviral actions of catechin can be partially explained.