Studies of Methane Monooxygenase and Alkane Oxidation Model Complexes
暂无分享,去创建一个
[1] G. Papaefthymiou,et al. Synthesis, structure, and electronic characterization of reactive diiron(II) 1,2-bis(2-hydroxybenzamido)benzene complexes as models for methane monooxygenase , 1991 .
[2] S. Lippard,et al. Redox properties of the hydroxylase component of methane monooxygenase from Methylococcus capsulatus (Bath). Effects of protein B, reductase, and substrate. , 1991, The Journal of biological chemistry.
[3] B. Fox,et al. Complex formation between the protein components of methane monooxygenase from Methylosinus trichosporium OB3b. Identification of sites of component interaction. , 1991, Journal of Biological Chemistry.
[4] Shih‐Yuan Liu,et al. MODELS OF THE REDUCED FORMS OF POLYIRON-OXO PROTEINS : AN ASYMMETRIC, TRIPLY CARBOXYLATE BRIDGED DIIRON(II) COMPLEX AND ITS REACTION WITH DIOXYGEN , 1991 .
[5] J. Vincent,et al. Proteins Containing Oxo-Bridged Dinuclear Iron Centers: A Bioinorganic Perspective , 1990 .
[6] G. Salmond,et al. Identification of the gene encoding the regulatory protein B of soluble methane monooxygenase , 1990 .
[7] Y. Mizutani,et al. Synthetic model for dioxygen binding sites of non-heme iron proteins. X-ray structure of Fe(OBz)(MeCN)[HB(3,5-iso-Pr2pz)3] [HB(3,5-iso-Pr2pz)3 = hydrotris(3,5-diisopropyl-1-pyrazolyl)borate] and resonance Raman evidence for reversible formation of a peroxo adduct , 1990 .
[8] D. T. Sawyer,et al. Redox chemistry of iron picolinate complexes and of their hydrogen peroxide and dioxygen adducts , 1990 .
[9] D. Kurtz. Oxo- and hydroxo-bridged diiron complexes: a chemical perspective on a biological unit , 1990 .
[10] L. Que,et al. Models for iron-oxo proteins: dioxygen binding to a diferrous complex , 1990 .
[11] G. Salmond,et al. The methane monooxygenase gene cluster of Methylococcus capsulatus (Bath). , 1990, Gene.
[12] H. Dalton,et al. Substrate specificity of soluble methane monooxygenase. Mechanistic implications. , 1989, The Journal of biological chemistry.
[13] 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.
[14] L. Que,et al. A (μ-oxo)(μ-carboxylato)diiron(III) complex with distinct iron sites , 1989 .
[15] D. Hendrickson,et al. Magnetic exchange interactions in semiquinone complexes of iron: structural and magnetic properties of tris(3,5-di-tert-butylsemiquinonato)iron(III) and tetrakis(3,5-di-tert-butylsemiquinonato)tetrakis(3,5-di-tert-butylcatecholato)tetrairon(III) , 1989 .
[16] S. Lippard,et al. Self assembly and dioxygen reactivity of an asymmetric, triply bridged diiron(II) complex with imidazole ligands and an open coordination site , 1989 .
[17] S. Lippard,et al. Characterization of a novel .mu.4-peroxide tetrairon unit of possible relevance to intermediates in metal-catalyzed oxidations of water to dioxygen , 1989 .
[18] M. Nanny,et al. Modeling the dinuclear sites of iron biomolecules: synthesis and properties of Fe2O(OAc)2Cl2(bipy)2 and its use as an alkane activation catalyst , 1988 .
[19] 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.
[20] L. Que,et al. Iron-oxo aggregates. Binuclear and tetranuclear complexes of N,N,N',N'-tetrakis(2-benzimidazolylmethyl)-2-hydroxy-1,3-diaminopropane , 1988 .
[21] 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 .
[22] L. Que,et al. Models for the iron(II)iron(III) and iron(II)iron(II) forms of iron-oxo proteins , 1988 .
[23] Y. Moro-oka,et al. A model for methane mono-oxygenase: dioxygen oxidation of alkanes by use of a µ-oxo binuclear iron complex , 1988 .
[24] D. Barton,et al. Functionalisation of saturated hydrocarbons. part x.1 a comparative study of chemical and electrochemical processes (gif and gif-orsay systems) in pyridine in acetone and in pyridine-co-solvent mixtures , 1988 .
[25] R. Prince,et al. Spectroscopic properties of the hydroxylase of methane monooxygenase. , 1988, Biochimica et biophysica acta.
[26] K. Hodgson,et al. EXAFS studies of binuclear iron complexes as models for hemerythrin and related proteins , 1986 .
[27] L. Que,et al. A binuclear iron peroxide complex capable of olefin epoxidation , 1986 .
[28] F. Arena,et al. A mixed valence µ-oxo iron(III)–iron(II) complex: a polynuclear iron–sodium–oxo aggregate from the chemical reduction of a µ-oxo di-iron(III) complex , 1986 .
[29] 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.
[30] D. Barton,et al. On the mechanism of the gif system for the oxidation of saturated hydrocarbons , 1985 .
[31] H. Dalton,et al. Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath). , 1985, European journal of biochemistry.
[32] D. Leak,et al. Mechanistic Studies on the Mode of Action of Methane Monooxygenase , 1985 .
[33] R. Frankel,et al. Assembly and characterization of an accurate model for the diiron center in hemerythrin , 1984 .
[34] S. Lippard,et al. Reversible protonation of the oxo bridge in a hemerythrin model compound. Synthesis, structure, and properties of (.mu.-hydroxo)bis(.mu.-acetato)bis[hydrotris(1-pyrazolyl)borato]diiron(III) [(HB(pz)3)Fe(OH)(O2CCH3)2Fe(HB(pz)3)2]+ , 1984 .
[35] J. Groves,et al. Hydroxylation by cytochrome P-450 and metalloporphyrin models: evidence for allylic rearrangement , 1984 .
[36] J. Groves,et al. Aliphatic hydroxylation catalyzed by iron porphyrin complexes , 1983 .
[37] K. Murray,et al. Iron complexes of N-substituted thiosalicylideneimines. Part 1. Synthesis and reactions with oxygen and carbon monoxide , 1983 .
[38] C. Anthony,et al. The Biochemistry of Methylotrophs , 1982 .
[39] D. Shriver,et al. Raman and infrared spectroscopy of the oxo-bridged iron(III) complex, [Cl3Fe-O-FeCl3]-2 as a spectroscopic model for the oxo bridge in hemerythrin and ribonucleotide reductase. , 1982, Journal of inorganic biochemistry.
[40] T. Spiro. Metal ion activation of dioxygen , 1980 .
[41] H. Dalton. Oxidation of Hydrocarbons by Methane Monooxygenases from a Variety of Microbes , 1980 .
[42] 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.
[43] C. Jefcoate,et al. Hydroxylation. Part IV. Oxidation of some benzenoid compounds by Fenton's reagent and the ultraviolet irradiation of hydrogen peroxide , 1969 .
[44] G. A. Hamilton,et al. Oxidation by Molecular Oxygen. I. Reactions of a Possible Model System for Mixed-Function Oxidases , 1964 .