Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath).
The azido complex formed in oxidized methane monooxygenase from Methylococcus capsulatus (Bath) was investigated with resonance Raman and FTIR techniques. These experiments show the presence of a nuas(NNN) at approximately 2077 cm-1 which splits to two components at 2059 and 2073 cm-1 with 15N14N2. The vibrational data are assigned to an azido complex bound terminally to one iron(III) at the diiron center. When the azido complex is illuminated at 15 K, a new nuas(NNN) is observed at 2136 cm-1 which is assigned to a photodissociated HN3 within the substrate pocket. We propose a model where an aqua ligand engages a hydrogen bond interaction with the 1N atom of the azido group and acts as at a proton donor during the photolysis process.
Lu
Shen
S
Department of Environmental & Biomolecular Systems, OGI School of Science & Engineering, Oregon Health & Science University, Beaverton, Oregon 97006-8921, USA.
Sazinsky
Matthew H
MH
Whittaker
James W
JW
Lippard
Stephen J
SJ
Moënne-Loccoz
Pierre
P
D001386:Azides / Q000737:chemistry*; D006860:Hydrogen Bonding; D020619:Methylococcus capsulatus / Q000201:enzymology*; D010105:Oxygenases / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
D001386:Azides; D010105:Oxygenases; C021555:methane monooxygenase