Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins
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Author(s)
Do, Loi Hung
Hayashi, Takahiro
Moenne-Loccoz, Pierre
Lippard, Stephen J.
Date Issued
January 2010
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society
Citation
Do, Loi H. et al. “Carboxylate as the Protonation Site in (Peroxo)diiron(III) Model Complexes of Soluble Methane Monooxygenase and Related Diiron Proteins.” Journal of the American Chemical Society 132.4 (2010) : 1273-1275.
Version
Author's final manuscript
Abstract
Dioxygen activation by carboxylate-bridged diiron enzymes
is involved in essential biological processes ranging from DNA
synthesis and hydrocarbon metabolism to cell proliferation.1-3
The carboxylate-bridged diiron superfamily of proteins includes
ribonucleotide reductase (RNR),4 Δ9 desaturase,5 bacterial
multicomponent monooxygenases (BMMs),6,7 and most recently
human deoxyhypusine hydroxylase (hDOHH).3 In all of these
systems, the O2 reduction step proceeds through a (peroxo)-
diiron(III) intermediate in which the resulting peroxo ligand is
proposed to bridge two iron atoms in a μ-1,2 or μ-η2η2
coordination mode.8-10 Extensive studies of soluble methane
monooxygenase (sMMO), a BMM family member that oxidizes
methane to methanol, reveal that the generation and activation
of Fe2O2 units requires protons.11,12 Given the complexity of
protein environments, identifying the sites involved in such
proton translocation processes and their effect on O2 activation
is not a trivial undertaking.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1021/ja909718f
