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

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

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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 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.

Original languageEnglish (US)
Pages (from-to)4148-4149
Number of pages2
JournalJournal of the American Chemical Society
Volume127
Issue number12
DOIs
StatePublished - Mar 30 2005

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methane monooxygenase
Methylococcus capsulatus
Photolysis
Fourier Analysis
Fourier Transform Infrared Spectroscopy
Baths
Protons
Hydrogen
Fourier transforms
Hydrogen bonds
Methane
Iron
Ligands
Infrared radiation
Atoms
Substrates
Experiments

ASJC Scopus subject areas

  • Chemistry(all)

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Fourier transform infrared characterization of the azido complex of methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath). / Lu, Shen; Sazinsky, Matthew H.; Whittaker, James; Lippard, Stephen J.; Moenne-Loccoz, Pierre.

In: Journal of the American Chemical Society, Vol. 127, No. 12, 30.03.2005, p. 4148-4149.

Research output: Contribution to journalArticle

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