Tuning the MnII2/MnIII2 redox cycle of a phenoxo-bridged diMn catalase mimic with terminal carboxylate donors. Solís, V., Palopoli, C., Daier, V., Rivière, E., Collin, F., Moreno, D. M., Hureau, C., & Signorella, S. Journal of Inorganic Biochemistry, 182:29–36, 2018. Paper doi abstract bibtex A new phenoxo-bridged diMnIII complex, Na[Mn2L(OH)2(H2O)2]·5H2O (1), obtained with the ligand L5− = 5‑methyl‑2‑hydroxo‑1,3‑xylene‑α,α‑diamine‑N,N,N′,N′‑tetraacetato, has been prepared and characterized. Mass spectrometry, conductivity, UV–visible, EPR and 1H NMR spectroscopic studies showed that the complex exists in solution as a monoanionic diMnIII complex. Complex 1 catalyzes H2O2 disproportionation with second-order rate constant kcat = 305(9) M−1 min−1 and without a time-lag phase. Based on spectroscopic results, the catalase activity of complex 1 in methanol involves a MnIII2/MnII2 redox cycle, which distinguishes this catalyst from other phenoxo-bridged diMn complexes that cycle between MnIIMnIII/MnIIIMnIV species. Addition of base stabilizes the catalyst, restrains demetallation during catalysis and causes moderate enhancement of catalase activity. The terminal carboxylate donors of 1 not only contribute as internal bases to assist deprotonation of H2O2 but also favor the formation of active homovalent diMn species, just as observed for the enzyme.
@article{solis_tuning_2018,
title = {Tuning the {MnII2}/{MnIII2} redox cycle of a phenoxo-bridged {diMn} catalase mimic with terminal carboxylate donors},
volume = {182},
issn = {0162-0134},
url = {https://www.sciencedirect.com/science/article/pii/S0162013417307389},
doi = {10.1016/j.jinorgbio.2018.01.013},
abstract = {A new phenoxo-bridged diMnIII complex, Na[Mn2L(OH)2(H2O)2]·5H2O (1), obtained with the ligand L5− = 5‑methyl‑2‑hydroxo‑1,3‑xylene‑α,α‑diamine‑N,N,N′,N′‑tetraacetato, has been prepared and characterized. Mass spectrometry, conductivity, UV–visible, EPR and 1H NMR spectroscopic studies showed that the complex exists in solution as a monoanionic diMnIII complex. Complex 1 catalyzes H2O2 disproportionation with second-order rate constant kcat = 305(9) M−1 min−1 and without a time-lag phase. Based on spectroscopic results, the catalase activity of complex 1 in methanol involves a MnIII2/MnII2 redox cycle, which distinguishes this catalyst from other phenoxo-bridged diMn complexes that cycle between MnIIMnIII/MnIIIMnIV species. Addition of base stabilizes the catalyst, restrains demetallation during catalysis and causes moderate enhancement of catalase activity. The terminal carboxylate donors of 1 not only contribute as internal bases to assist deprotonation of H2O2 but also favor the formation of active homovalent diMn species, just as observed for the enzyme.},
language = {en},
urldate = {2022-02-01},
journal = {Journal of Inorganic Biochemistry},
author = {Solís, Verónica and Palopoli, Claudia and Daier, Verónica and Rivière, Eric and Collin, Fabrice and Moreno, Diego M. and Hureau, Christelle and Signorella, Sandra},
year = {2018},
pages = {29--36},
}
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Mass spectrometry, conductivity, UV–visible, EPR and 1H NMR spectroscopic studies showed that the complex exists in solution as a monoanionic diMnIII complex. Complex 1 catalyzes H2O2 disproportionation with second-order rate constant kcat = 305(9) M−1 min−1 and without a time-lag phase. Based on spectroscopic results, the catalase activity of complex 1 in methanol involves a MnIII2/MnII2 redox cycle, which distinguishes this catalyst from other phenoxo-bridged diMn complexes that cycle between MnIIMnIII/MnIIIMnIV species. Addition of base stabilizes the catalyst, restrains demetallation during catalysis and causes moderate enhancement of catalase activity. The terminal carboxylate donors of 1 not only contribute as internal bases to assist deprotonation of H2O2 but also favor the formation of active homovalent diMn species, just as observed for the enzyme.","language":"en","urldate":"2022-02-01","journal":"Journal of Inorganic Biochemistry","author":[{"propositions":[],"lastnames":["Solís"],"firstnames":["Verónica"],"suffixes":[]},{"propositions":[],"lastnames":["Palopoli"],"firstnames":["Claudia"],"suffixes":[]},{"propositions":[],"lastnames":["Daier"],"firstnames":["Verónica"],"suffixes":[]},{"propositions":[],"lastnames":["Rivière"],"firstnames":["Eric"],"suffixes":[]},{"propositions":[],"lastnames":["Collin"],"firstnames":["Fabrice"],"suffixes":[]},{"propositions":[],"lastnames":["Moreno"],"firstnames":["Diego","M."],"suffixes":[]},{"propositions":[],"lastnames":["Hureau"],"firstnames":["Christelle"],"suffixes":[]},{"propositions":[],"lastnames":["Signorella"],"firstnames":["Sandra"],"suffixes":[]}],"year":"2018","pages":"29–36","bibtex":"@article{solis_tuning_2018,\n\ttitle = {Tuning the {MnII2}/{MnIII2} redox cycle of a phenoxo-bridged {diMn} catalase mimic with terminal carboxylate donors},\n\tvolume = {182},\n\tissn = {0162-0134},\n\turl = {https://www.sciencedirect.com/science/article/pii/S0162013417307389},\n\tdoi = {10.1016/j.jinorgbio.2018.01.013},\n\tabstract = {A new phenoxo-bridged diMnIII complex, Na[Mn2L(OH)2(H2O)2]·5H2O (1), obtained with the ligand L5− = 5‑methyl‑2‑hydroxo‑1,3‑xylene‑α,α‑diamine‑N,N,N′,N′‑tetraacetato, has been prepared and characterized. Mass spectrometry, conductivity, UV–visible, EPR and 1H NMR spectroscopic studies showed that the complex exists in solution as a monoanionic diMnIII complex. Complex 1 catalyzes H2O2 disproportionation with second-order rate constant kcat = 305(9) M−1 min−1 and without a time-lag phase. Based on spectroscopic results, the catalase activity of complex 1 in methanol involves a MnIII2/MnII2 redox cycle, which distinguishes this catalyst from other phenoxo-bridged diMn complexes that cycle between MnIIMnIII/MnIIIMnIV species. Addition of base stabilizes the catalyst, restrains demetallation during catalysis and causes moderate enhancement of catalase activity. The terminal carboxylate donors of 1 not only contribute as internal bases to assist deprotonation of H2O2 but also favor the formation of active homovalent diMn species, just as observed for the enzyme.},\n\tlanguage = {en},\n\turldate = {2022-02-01},\n\tjournal = {Journal of Inorganic Biochemistry},\n\tauthor = {Solís, Verónica and Palopoli, Claudia and Daier, Verónica and Rivière, Eric and Collin, Fabrice and Moreno, Diego M. and Hureau, Christelle and Signorella, Sandra},\n\tyear = {2018},\n\tpages = {29--36},\n}\n\n","author_short":["Solís, V.","Palopoli, C.","Daier, V.","Rivière, E.","Collin, F.","Moreno, D. 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