We examined the static and dynamic characters of the red luminescence in the protein-Au(III) compounds, directly comparing multiple proteins: BSA, OVA, trypsin, and insulin. These four protein-Au(III) complexes showed a nearly identical excitation-emission pattern, not only the wavelength of luminescence (λem ∼ 640 nm). Lifetimes of the red luminescence shared a common value of ∼300 ns. Kinetics of the luminophore formation was consistently described by a Langmuir-type chemisorption of Au(III) for these proteins, coinciding with the protein conformation change at pH ∼ 10. These observations and the protein structural analyses support that the red luminophore formation involves Au(III) coordination to a common motif within these proteins.