Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction.

[1]  B. Fox,et al.  Haloalkene oxidation by the soluble methane monooxygenase from Methylosinus trichosporium OB3b: mechanistic and environmental implications. , 1990, Biochemistry.

[2]  P A Frey,et al.  Methane monooxygenase catalyzed oxygenation of 1,1-dimethylcyclopropane. Evidence for radical and carbocationic intermediates. , 1990, Biochemistry.

[3]  L. Wackett,et al.  Biodegradation of trichloroethylene by Methylosinus trichosporium OB3b , 1989, Applied and environmental microbiology.

[4]  B. Fox,et al.  Methane monooxygenase from Methylosinus trichosporium OB3b. Purification and properties of a three-component system with high specific activity from a type II methanotroph. , 1989, The Journal of biological chemistry.

[5]  D. Rees,et al.  Cross-linking of nitrogenase components. Structure and activity of the covalent complex. , 1989, The Journal of biological chemistry.

[6]  L. Que,et al.  Mössbauer and EPR studies of the binuclear iron center in ribonucleotide reductase from Escherichia coli. A new iron-to-protein stoichiometry. , 1989, The Journal of biological chemistry.

[7]  H. Dalton,et al.  A stopped-flow kinetic study of soluble methane mono-oxygenase from Methylococcus capsulatus (Bath). , 1989, The Biochemical journal.

[8]  B. Fox,et al.  Evidence for a mu-oxo-bridged binuclear iron cluster in the hydroxylase component of methane monooxygenase. Mössbauer and EPR studies. , 1988, The Journal of biological chemistry.

[9]  B. Fox,et al.  Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph. , 1988, Biochemical and biophysical research communications.

[10]  K. Hodgson,et al.  Structural characterization by EXAFS spectroscopy of the binuclear iron center in protein A of methane monooxygenase from Methylococcus capsulatus (Bath) , 1988 .

[11]  P. Debrunner,et al.  Reduction of the binuclear iron site in octameric methemerythrins. Characterizations of intermediates and a unifying reaction scheme , 1987 .

[12]  R. Patel,et al.  Purification and properties of the hydroxylase component of methane monooxygenase , 1987, Journal of bacteriology.

[13]  R. Cammack,et al.  ESR studies of protein A of the soluble methane monooxygenase from Methylococcus capsulatus (Bath) , 1986 .

[14]  L. Que,et al.  The interaction of phosphate with uteroferrin. Characterization of a reduced uteroferrin-phosphate complex. , 1986, The Journal of biological chemistry.

[15]  R. W. Wright,et al.  Enhancement by N-hydroxysulfosuccinimide of water-soluble carbodiimide-mediated coupling reactions. , 1986, Analytical biochemistry.

[16]  B. Guigliarelli,et al.  An analysis of the g values in semi-met forms of hemerythrin and in related proteins. , 1986, Archives of biochemistry and biophysics.

[17]  H. Dalton,et al.  Protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). A novel regulatory protein of enzyme activity. , 1985, The Journal of biological chemistry.

[18]  M. Hendrich,et al.  Chloroperoxidase compound I: Electron paramagnetic resonance and Mössbauer studies. , 1984, Biochemistry.

[19]  D. Scott,et al.  Substrate Specificities of the Soluble and Particulate Methane Mono-oxygenases of Methylosinus trichosporium OB3b , 1984 .

[20]  H. S. Mason,et al.  Oxidases and Related Redox Systems , 1982 .

[21]  J D Lipscomb,et al.  Electron paramagnetic resonance detectable states of cytochrome P-450cam. , 1980, Biochemistry.

[22]  H. Dalton,et al.  Resolution of the methane mono-oxygenase of Methylococcus capsulatus (Bath) into three components. Purification and properties of component C, a flavoprotein. , 1978, The Biochemical journal.

[23]  S. Sligar,et al.  A thermodynamic model of regulation: modulation of redox equilibria in camphor monoxygenase. , 1976, Proceedings of the National Academy of Sciences of the United States of America.

[24]  T. Vänngård,et al.  EPR signal intensity and powder shapes: A reexamination , 1975 .

[25]  S. Sligar,et al.  A role of the putidaredoxin COOH-terminus in P-450cam (cytochrome m) hydroxylations. , 1974, Proceedings of the National Academy of Sciences of the United States of America.

[26]  B. Fox,et al.  Integer-spin EPR studies of the fully reduced methane monooxygenase hydroxylase component , 1990 .

[27]  B. Fox,et al.  Methane monooxygenase from Methylosinus trichosporium OB3b. , 1990, Methods in enzymology.

[28]  R. Prince,et al.  Spectroscopic properties of the hydroxylase of methane monooxygenase. , 1988, Biochimica et biophysica acta.

[29]  R. S. Hanson Ecology and Diversity of Methylotrophic Organisms , 1980 .

[30]  H. Dalton Oxidation of Hydrocarbons by Methane Monooxygenases from a Variety of Microbes , 1980 .