Synthetic biology pursues the understanding of biological processes and their possible mimicry with artificial bioinspired materials. A number of materials have already been used to mimic the active site of simple redox proteins, including nanosized iron oxides due to their redox properties. However, the mimicry of membrane redox protein complexes is still a challenge. Herein, magnetic iron oxide nanoparticles (NPs), incorporated as non-proteinaceous complexes III and IV in a mitochondrial model membrane, catalyze electron transfer (ET) similarly to the natural complexes towards cytochrome c. The associated molecular mechanism is experimentally proven in solution and in a Langmuir-Blodgett film. A direct and entropy-driven ET, with rate constant of 2.63 ± 0.05Lmol-1 at 25 °C, occurs between the iron sites of the NPs and the cytochrome c heme group, not affecting the protein secondary and tertiary structures. This process requires an activation energy of 40.2 ± 1.5 kJ mol-1 resulting in an overall Gibbs free energy of -55.3 kJ mol-1. Furthermore, the protein-NP system is governed by electrostatic and non-polar forces that contribute to an associative mechanism in the transition state. Finally, the incorporated NPs in a model membrane were able to catalyze ET, such as the natural complexes in respiratory chain. This work presents an experimental approach demonstrating that inorganic nanostructured systems may behave as embedded proteins in the eukaryotic cells membrane, opening the way for more sophisticated and robust mimicry of membrane protein complexes.