A potential candidate for an oxygen-sensing protein in chemoreceptor cells is a heme-linked multicomponent NADPH oxidase, originally described in neutrophils. The postulated function for the oxidase in chemoreceptor cells is to signal changes in oxygen levels (either in the blood or in the airway lumen) via changes in oxygen metabolite production. An alteration in either superoxide (or dismuted hydrogen peroxide) production may affect the gating properties of the O 2 -sensitive K 1 channels. We have previously reported immunohistochemical localization of gp91 glycoprotein component of the oxidase to the plasma membrane of pulmonary neuroepithelial body (NEB) cells. In this study we have investigated the immunocytochemical localization of the other polypeptide components of the oxidase in NEB cells and in the glomus cells of the carotid body. Cultures of dissociated fetal rabbit NEB cells and newborn rat glomus cells were immunostained with specific antibodies recognizing the various polypeptide subunits of the oxidase using indirect immunofluorescence methods. Immunostaining with the anti-oxidase antibodies revealed strong positive reaction in both NEB and glomus cell clusters while other cells were unstained. The positive reaction product was localized to the plasma membrane and/or cytoplasm and no nuclear staining was observed. Live cell labelling studies with anti-p22 antibody showed positive immunofluorescence on the surface of NEB cells, suggesting that this component of the oxidase is also associated with the plasma membrane. In glomus cells, similar strongly positive immunofluorescence signal was observed for p22 and gp91 in paraformaldehyde-fixed cultures, regardless whether they were permeabilized or not. Taken together, our findings of cell surface localization of gp91 and p22 components of the oxidase in chemoreceptive cells suggests that the heme-linked cytochrome b 558 component is associated with the plasma membrane. This association allows for direct interaction with the O 2 -sensitive K 1 channel thus forming the molecular complex of membrane bound O 2 sensor.