Heme c is characterized by its covalent attachment to a polypeptide. The attachment is typically to a CXXCH motif in which the two Cys form thioether bonds with the heme, “X” can be any amino acid other than Cys, and the His serves as a heme axial ligand. Some cytochromes c, however, contain heme attachment motifs with three or four intervening residues in a CX3CH or CX4CH motif. Here, the impacts of these variations in the heme attachment motif on heme rufing and electronic structure are investigated by spectroscopically characterizing CX3CH and CX4CH variants of Hydrogenobacter thermophilus cytochrome c552. In addition, a novel CXCH variant is studied. 1 H and 13C NMR, EPR, and resonance Raman spectra of the protein variants are analyzed to deduce the extent of rufing using previously reported relationships between these spectral data and heme rufing. In addition, the reduction potentials of these protein variants are measured using protein flm voltammetry. The CXCH and CX4CH variants are found to have enhanced heme rufing and lower reduction potentials. Implications of these results for the use of these noncanonical motifs in nature, and for the engineering of novel heme peptide structures, are discussed.