The pathogenic Neisseria spp. are capable of iron utilization from host iron‐binding proteins including transferrin and lactoferrin. Transferrin iron utilization is an energy‐dependent, receptor‐mediated event in which two identified transferrin‐binding proteins participate. One of these proteins, TbpA, is homologous to the TonB‐dependent family of outer membrane receptors that are required for high‐affinity uptake of vitamin B₁₂ and ferric siderophores. The ‘TonB box’ is a conserved domain near the amino‐terminus of these proteins that has been implicated in interaction with TonB. Interaction between a periplasmic domain of TonB and the TonB box allows energy transduction to occur from the cytoplasmic membrane to the energy‐dependent receptor in the outer membrane. We created a TonB box mutant of gonococcal TbpA and demonstrated that its binding and protease accessibility characteristics were indistinguishable from those of gonococcal Ton system mutants. The protease exposure of the second transferrin‐binding protein, TbpB, was affected by the energization of TbpA, consistent with an interaction between these proteins. TbpB expressed by the de‐energized mutants was readily accessible to protease, similar to TbpB expressed in the absence of TbpA. The de‐energized mutants exhibited a marked decrease in transferrin diffusion rate, suggesting that receptor energization was necessary for ligand release. We propose a model to explain the observed Ton‐dependent changes in the binding parameters and exposures of TbpA and TbpB.