Carboxylate as the protonation site in (peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins

Loi H. Do; Takahiro Hayashi; Pierre Moënne-Loccoz; Stephen J. Lippard

doi:10.1021/ja909718f

Carboxylate as the protonation site in (peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins

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

Chemical Physiology and Biochemistry

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

Abstract

(Chemical Equation Presented) Addition of H⁺ to a synthetic (μ-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, ⁵⁷Fe Mössbauer, resonance Raman, infrared, and ¹H/¹⁹F 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.

Original language	English (US)
Pages (from-to)	1273-1275
Number of pages	3
Journal	Journal of the American Chemical Society
Volume	132
Issue number	4
DOIs	https://doi.org/10.1021/ja909718f
State	Published - Feb 3 2010

ASJC Scopus subject areas

Catalysis
Chemistry(all)
Biochemistry
Colloid and Surface Chemistry

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AU - Do, Loi H.

AU - Hayashi, Takahiro

AU - Moënne-Loccoz, Pierre

AU - Lippard, Stephen J.

PY - 2010/2/3

Y1 - 2010/2/3

N2 - (Chemical Equation Presented) Addition of H+ to a synthetic (μ-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, 57Fe Mössbauer, resonance Raman, infrared, and 1H/19F 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.

AB - (Chemical Equation Presented) Addition of H+ to a synthetic (μ-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, 57Fe Mössbauer, resonance Raman, infrared, and 1H/19F 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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Carboxylate as the protonation site in (peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins

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