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

Research output: Contribution to journalArticlepeer-review

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 languageEnglish (US)
Pages (from-to)1273-1275
Number of pages3
JournalJournal of the American Chemical Society
Volume132
Issue number4
DOIs
StatePublished - Feb 3 2010

Funding

FundersFunder number
Author National Institutes of Health National Institutes of Health National Institutes of Health National Institutes of Health The Bev Hartig Huntington's Disease Foundation National Institutes of Health
National Institute of General Medical SciencesR37GM032134

    ASJC Scopus subject areas

    • Catalysis
    • General Chemistry
    • Biochemistry
    • Colloid and Surface Chemistry

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