Spectroscopic properties of the hydroxylase of methane monooxygenase.
The hydroxylase component of methane monooxygenase (EC 1.14.13.25), which catalyzes the oxidation of methane to methanol, has been studied by visible, electron spin resonance and X-ray spectroscopies. The enzyme appears to possess a mu-oxo- or mu-hydroxo-bridged binuclear iron site, with no sulfur ligands to the cluster. Each Fe has 4-6 oxygen (or nitrogen) ligands, at an average distance of 1.92 +/- 0.03 A. The Fe-Fe distance is 3.05 +/- 0.05 A. Essentially all of the irons are in the Fe3+ state as the enzyme is prepared, but reduction with N-methylphenazonium methosulfate generates ESR-detectable states that appear to emanate from mixed-valence binuclear sites. One of these, with gav near 1.85, displays typical Curie law microwave saturation behavior, but the other, gav near 1.73, has a very potent method of spin-relaxation. Together they account for approximately 0.6 spins per molecule.
Prince
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Exxon Research and Engineering Co., Annandale, NJ 08801.
George
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Savas
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Cramer
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Patel
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D001665:Binding Sites; D004578:Electron Spin Resonance Spectroscopy; D019605:Euryarchaeota / Q000201:enzymology*; D007501:Iron / Q000032:analysis; D007700:Kinetics; D006899:Mixed Function Oxygenases; D010105:Oxygenases / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D013053:Spectrophotometry; D013057:Spectrum Analysis; D013816:Thermodynamics
D007501:Iron; D006899:Mixed Function Oxygenases; D010105:Oxygenases; C021555:methane monooxygenase