Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

Shen Lu; Matthew H. Sazinsky; James W. Whittaker; Stephen J. Lippard; Pierre Moënne-Loccoz

doi:10.1021/ja044414u

Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

Shen Lu, Matthew H. Sazinsky, James W. Whittaker, Stephen J. Lippard, Pierre Moënne-Loccoz

Chemical Physiology and Biochemistry

Research output: Contribution to journal › Article › peer-review

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Abstract

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 ν_as(NNN) at ∼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 ν_as(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.

Original language	English (US)
Pages (from-to)	4148-4149
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	12
DOIs	https://doi.org/10.1021/ja044414u
State	Published - Mar 30 2005

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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title = "Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)",

abstract = "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 νas(NNN) at ∼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 νas(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.",

author = "Shen Lu and Sazinsky, {Matthew H.} and Whittaker, {James W.} and Lippard, {Stephen J.} and Pierre Mo{\"e}nne-Loccoz",

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T1 - Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

AU - Lu, Shen

AU - Sazinsky, Matthew H.

AU - Whittaker, James W.

AU - Lippard, Stephen J.

AU - Moënne-Loccoz, Pierre

PY - 2005/3/30

Y1 - 2005/3/30

N2 - 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 νas(NNN) at ∼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 νas(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.

AB - 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 νas(NNN) at ∼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 νas(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.

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Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath)

Abstract

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