Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.
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ABSTRACT:
SUBMITTER: Do LH
PROVIDER: S-EPMC2812653 | biostudies-literature | 2010 Feb
REPOSITORIES: biostudies-literature
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Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.
Do Loi H LH Hayashi Takahiro T Moënne-Loccoz Pierre P Lippard Stephen J SJ
Journal of the American Chemical Society 20100201 4
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. ...[more]
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