Carboxylate as the protonation site in (Peroxo)diiron(III) model complexes of soluble methane monooxygenase and related diiron proteins.
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.
Do
Loi H
LH
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Hayashi
Takahiro
T
Moënne-Loccoz
Pierre
P
Lippard
Stephen J
SJ
D002264:Carboxylic Acids / Q000737:chemistry*; D020134:Catalytic Domain; D005290:Ferric Compounds / Q000737:chemistry*; D008954:Models, Biological; D010100:Oxygen / Q000737:chemistry*; D010105:Oxygenases / Q000737:chemistry*; D011522:Protons
D002264:Carboxylic Acids; D005290:Ferric Compounds; D011522:Protons; D010105:Oxygenases; C021555:methane monooxygenase; D010100:Oxygen