Iron-sulfur clusters are common building blocks for electron transport and active sites of metalloproteins. Their comprehensive investigation is crucial for understanding these enzymes, which play important roles in modern biomimetic catalysis and biotechnology applications. We address this issue by utilizing (Et₄N)₃[Fe₄Te₄(SPh)₄], a tellurium modified version of a conventional reduced [4Fe-4S]⁺ cluster, and performed both ⁵⁷Fe- and ¹²⁵Te-NRVS to reveal its characteristic vibrational features. Our analysis exposed major differences in the resulting ⁵⁷Fe spectrum profile as compared to that of the respective [4Fe-4S] cluster, and between the ⁵⁷Fe and ¹²⁵Te profiles. DFT calculations are applied to rationalize structural, electronic, vibrational, and redox-dependent properties of the [4Fe-4Te]⁺ core. We herein highlight the potential of sulfur/tellurium exchange as a method to isolate the iron-only motion in enzymatic systems.