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Model of the MitoNEET [2Fe−2S] Cluster Shows Proton Coupled Electron Transfer

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Institute of Inorganic Chemistry, Georg-August-University Göttingen, Tammannstraße 4, D-37077 Göttingen, Germany
Yale University, 225 Prospect Street, New Haven, Connecticut 06511, United States
Cite this: J. Am. Chem. Soc. 2017, 139, 2, 701–707
Publication Date (Web):January 5, 2017
https://doi.org/10.1021/jacs.6b09180
Copyright © 2017 American Chemical Society

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    Abstract

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    MitoNEET is an outer membrane protein whose exact function remains unclear, though a role of this protein in redox and iron sensing as well as in controlling maximum mitochondrial respiratory rates has been discussed. It was shown to contain a redox active and acid labile [2Fe–2S] cluster which is ligated by one histidine and three cysteine residues. Herein we present the first synthetic analogue with biomimetic {SN/S2} ligation which could be structurally characterized in its diferric form, 52–. In addition to being a high fidelity structural model for the biological cofactor, the complex is shown to mediate proton coupled electron transfer (PCET) at the {SN} ligated site, pointing at a potential functional role of the enzyme’s unique His ligand. Full PCET thermodynamic square schemes for the mitoNEET model 52– and a related homoleptic {SN/SN} capped [2Fe–2S] cluster 42– are established, and kinetics of PCET reactivity are investigated by double-mixing stopped-flow experiments for both complexes. While the N—H bond dissociation free energy (BDFE) of 5H2– (230 ± 4 kJ mol–1) and the free energy ΔG°PCET for the reaction with TEMPO (−48.4 kJ mol–1) are very similar to values for the homoleptic cluster 4H2– (232 ± 4 kJ mol–1, –46.3 kJ mol–1) the latter is found to react significantly faster than the mitoNEET model (data for 5H2–: k = 135 ± 27 M–1 s–1, ΔH = 17.6 ± 3.0 kJ mol–1, ΔS = −143 ± 11 J mol–1 K–1, and ΔG = 59.8 kJ mol–1 at 293 K). Comparison of the PCET efficiency of these clusters emphasizes the relevance of reorganization energy in this process.

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    The Supporting Information is available free of charge on the ACS Publications website at DOI: 10.1021/jacs.6b09180.

    • Synthetic procedures, full experimental details, 1H NMR and UV–vis titrations, additional Mößbauer spectra, details of kinetic investigations, and details of magnetic measurements (PDF)

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