Oxidation-reduction potentials of the methane monooxygenase hydroxylase component from Methylosinus trichosporium OB3b

Methane monooxygenase (MMO) isolated from Methylosinus trichosporium OB3b consists of hydroxylase (MMOH), reductase (MMOR), and "B" (MMOB) protein components. MMOH contains two oxygen-bridged dinuclear iron clusters that are the sites of O2 activation and hydrocarbon oxidation. Each cluste...

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Bibliographic Details
Published in:	Biochemistry (Easton) Vol. 33; no. 3; pp. 713 - 722
Main Authors:	Paulsen, Kim E, Liu, Yi, Fox, Brian G, Lipscomb, John D, Munck, Eckard, Stankovich, Marian T
Format:	Journal Article
Language:	English
Published:	Washington, DC American Chemical Society 01-01-1994
Subjects:	Alkenes - chemistry Analytical, structural and metabolic biochemistry Biological and medical sciences Electron Spin Resonance Spectroscopy Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Mechanisms. Catalysis. Electron transfer. Models Methylococcaceae - enzymology Methylosinus trichosporium Models, Chemical Molecular biophysics Oxidation-Reduction Oxidoreductases Oxygenases - chemistry Physical chemistry in biology Potentiometry Thermodynamics Redox state Iron Complexes Methylosinus trichosporium Enzyme Association dissociation Reaction mechanism Bacteria Methane monooxygenase Oxidoreductases Redox potential Subunit Conformational transition
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