Moessbauer, EPR, and ENDOR studies of the hydroxylase and reductase components of methane monooxygenase from Methylosinus trichosporium OB3b
| Autor: | Eckard Münck, Kristoffer K. Andersson, Kristene K. Surerus, Brian G. Fox, Michael P. Hendrich, Wayne A. Froland, John D. Lipscomb |
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| Rok vydání: | 1993 |
| Předmět: |
biology
Chemistry Methane monooxygenase Stereochemistry Active site Methylosinus trichosporium General Chemistry Reductase Biochemistry Catalysis law.invention Colloid and Surface Chemistry law Mössbauer spectroscopy biology.protein Cluster (physics) Mossbauer spectra Electron paramagnetic resonance |
| Zdroj: | Journal of the American Chemical Society. 115:3688-3701 |
| ISSN: | 1520-5126 0002-7863 0553-1055 |
| Popis: | Soluble methane monooxygenase (MMO) isolated from Methylosinus trichosporium OB3b consists of three components: hydroxylase, reductase, and component B. The active-site diiron cluster of the hydroxylase has been studied with Mossbauer, ANDOR, and APR spectroscopies. Mossbauer spectra of the oxidized cluster show that the two high-spin irons are antiferromagnetically coupled in accord with our preliminary study (Fox et al. J. Biol. Chem. 1988, 263, 10553-10556). Mossbauer studies also reveal the presence of two cluster conformations at pH 9. The excited-state S=2 multiplet of the exchange-coupled cluster (Fe 3+ -Fe 3+ ) gives rise to an integer-spin EPR signal near g=8; this is the first quantitative study of such a signal from any system |
| Databáze: | OpenAIRE |
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