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2010•Journal of the American Chemical SocietyOpen access

Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins

Loi H., Takahiro Hayashi, Pierre Moënne‐Loccoz, Stephen J. Lippard

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Abstract

Addition of H(+) to a synthetic (mu-1,2-peroxo)diiron(III) model complex results in protonation of a carboxylate rather than the peroxo ligand. This conclusion is based on spectroscopic evidence from UV-vis, (57)Fe Mossbauer, resonance Raman, infrared, and (1)H/(19)F NMR studies. These results suggest a similar role for protons in the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged diiron enzymes.

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Addition of H(+) to a synthetic (mu-1,2-peroxo)diiron(III) model complex results in protonation of a carboxylate rather than the peroxo ligand. This conclusion is based on spectroscopic evidence from UV-vis, (57)Fe Mossbauer, resonance Raman, infrared, and (1)H/(19)F NMR studies. These results suggest a similar role for protons in the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged diiron enzymes.

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Available abstract

Addition of H(+) to a synthetic (mu-1,2-peroxo)diiron(III) model complex results in protonation of a carboxylate rather than the peroxo ligand. This conclusion is based on spectroscopic evidence from UV-vis, (57)Fe Mossbauer, resonance Raman, infrared, and (1)H/(19)F NMR studies. These results suggest a similar role for protons in the dioxygen activation reactions in soluble methane monooxygenase and related carboxylate-bridged diiron enzymes.

Key concepts: Chemistry, Methane monooxygenase, Protonation, Carboxylate, Methane, Monooxygenase, Photochemistry, Organic chemistry

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Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins — Research Paper | ScholarLens