Biological systems use copper as a redox center in many metalloproteins, where the role of the metal is to cycle between its +1 and +2 oxidation states. This chemistry requires the redox potential to be in a range that can stabilize both Cu(I) and Cu(II) states and often involves protein-derived ligand sets involving mixed histidine-methionine coordination that balance the preferences of both oxidation states. Transport proteins, on the other hand, utilize copper in the Cu(I) state and often contain sites comprised predominately of the cuprophilic residue methionine. The electtonic factors that allow enzymes and transporters to balance their redox requirements are complex and are often elusive due to the dearth of spectroscopic probes of the Cu(I) state. Here we present the novel application of X-ray emission spectroscopy to copper proteins via a study of a series of mixed His-Met copper sites where the ligand set varies in a systematic way between the His(3) and Met(3) limits. The sites are derived from the wild-type peptidylglycine monooxygenase (PHM), two single-site variants which replicate each of its two copper sites (Cu-M-site and Cu-H-site), and the transporters CusF and CusB. Clear differences are observed in the K beta(2,5) region at the Met(3) and His(3) limits. CusB (Met(3)) has a distinct peak at 8978.4 eV with a broad shoulder at 8975.6 eV, whereas Cu-H (His(3)) has two well-resolved features: a more intense feature at 8974.8 eV and a second at 8977.2 eV. The mixed coordination sphere CusF (Met(2)His) and the PHM Cu-M variant (Met(1)His(2)) have very similar spectra consisting of two features at 8975.2 and 8977.8 eV. An analysis of DFT calculated spectra indicate that the intensity of the higher energy peak near 8978 eV is mediated by mixing of ligand-based orbitals into the Cu d(10) manifold, with S from Met providing more intensity by facilitating increased Cu p-d mixing. Furthermore, reaction of WT PHM with CO (an oxygen analogue) produced the M site CO complex, which showed a unique XES spectrum that could be computationally reproduced by including interactions between Cu(I). and the CO ligand. The study suggests that the valence-to-core (VtC) region can not only serve as a probe of ligand speciation but also offer insight into the coordination geometry, in a fashion similar to XAS pre-edges, and may be sufficiently sensitive to the coordination of exogenous ligands to be useful in the study of reaction mechanisms.