57Fe Mössbauer Spectroscopy in Chemistry and Biology

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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wetenschappelijk artikel

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наукова стаття, опублікована у квітні 2010

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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57Fe Mössbauer Spectroscopy in Chemistry and Biology

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P1476

57Fe Mössbauer Spectroscopy in Chemistry and Biology

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P2093

Eckard Münck

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Marlène Martinho

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P2860

Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane

The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein

The Leeuwenhoek Lecture 2000 the natural and unnatural history of methane-oxidizing bacteria

Iron-sulfur clusters: nature's modular, multipurpose structures.

Rapid total destruction of chlorophenols by activated hydrogen peroxide.

Characterization of the particulate methane monooxygenase metal centers in multiple redox states by X-ray absorption spectroscopy

Iron-sulfur proteins: ancient structures, still full of surprises.

Biological methane oxidation: regulation, biochemistry, and active site structure of particulate methane monooxygenase.

Characterization and structural analysis of an active particulate methane monooxygenase trimer from Methylococcus capsulatus (Bath).

Purified particulate methane monooxygenase from Methylococcus capsulatus (Bath) is a dimer with both mononuclear copper and a copper-containing cluster.

P304

39-67

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P31

scholarly article

P356

10.1002/9780470602539.CH2

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P577

2010-04-22T00:00:00Z

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