Search Results - (Author, Cooperation:J. D. Lipscomb)
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1Latest Papers from Table of Contents or Articles in PressR. Banerjee ; Y. Proshlyakov ; J. D. Lipscomb ; D. A. Proshlyakov
Nature Publishing Group (NPG)
Published 2015Staff ViewPublication Date: 2015-01-22Publisher: Nature Publishing Group (NPG)Print ISSN: 0028-0836Electronic ISSN: 1476-4687Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsKeywords: Biocatalysis ; Biodegradation, Environmental ; Carbon/chemistry/metabolism ; Hydrogen/chemistry/metabolism ; Iron Compounds/*chemistry/metabolism ; Methane/*chemistry/*metabolism ; Methanol/*chemistry/*metabolism ; Oxidation-Reduction ; Oxygen/chemistry/metabolism ; Oxygen Isotopes ; Oxygenases/*metabolism ; Spectrum Analysis, Raman ; VibrationPublished by: -
2Articles: DFG German National LicensesGunsalus, I. C. ; Lipscomb, J. D. ; Meeks, J. R.
Oxford, UK : Blackwell Publishing Ltd
Published 1973Staff ViewISSN: 1749-6632Source: Blackwell Publishing Journal Backfiles 1879-2005Topics: Natural Sciences in GeneralType of Medium: Electronic ResourceURL: -
3Articles: DFG German National LicensesStaff View
ISSN: 1476-4687Source: Nature Archives 1869 - 2009Topics: BiologyChemistry and PharmacologyMedicineNatural Sciences in GeneralPhysicsNotes: [Auszug] The structure of 3,4-PCD was solved using a combination of isomorphous replacement and molecular averaging to produce the map in Fig. 1. This map shows continuous electron density for both chains and accounts for all but the first three and last two residues of the ft chain. The course of the ...Type of Medium: Electronic ResourceURL: -
4Articles: DFG German National LicensesStaff View
ISSN: 1432-1327Keywords: Key words Monooxygenase mechanism ; Oxygen activation ; Fe(IV) ; Compound Q ; Model complexesSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract Methane monooxygenase (MMO) catalyzes the oxidation of stable hydrocarbons that are not attacked by cytochrome P450 monooxygenase. A key transient intermediate in the catalytic cycle of the soluble form of MMO termed compound Q (Q) has been trapped and characterized through spectroscopic comparisons with novel high valent model complexes. Q appears to contain a non-heme dinuclear Fe(IV) cluster bridged by at least two single oxygen atoms to form a so-called diamond core. Q has the ability to react directly with unactivated hydrocarbons to yield oxidized products. Several types of experiments indicate that this reaction involves formation of an intermediate, probably with radical character. This is consistent with a hydrogen atom abstraction mechanism analogous to that ascribed to cytochrome P450. However, these same experiments show that a pure hydrogen atom abstraction mechanism is unlikely for many substrates without an additional interaction between the intermediate that is formed and the high valent cluster. The results may be of general relevance to monooxygenase catalysis.Type of Medium: Electronic ResourceURL: -
5Articles: DFG German National LicensesStaff View
ISSN: 1432-1327Keywords: Key words Methane monooxygenase ; EXAFS ; XANES ; Oxygen activationSource: Springer Online Journal Archives 1860-2000Topics: BiologyChemistry and PharmacologyNotes: Abstract The conversion from methane to methanol is catalyzed by methane monooxygenase (MMO) in methanotrophic bacteria. Earlier work on the crystal structures of the MMO hydroxylase component (MMOH) from Methylococcus capsulatus (Bath) at 4 °C and –160 °C has revealed two different core arrangements for the diiron active site. To ascertain the generality of these results, we have now carried out the first structural characterization on MMOH from Methylosinus trichosporium OB3b. Our X-ray absorption spectroscopic (XAS) analysis suggests the presence of two Fe-Fe distances of about 3 Å and 3.4 Å, which are proposed to reflect two populations of MMOH molecules with either a bis(μ-hydroxo)(μ-carboxylato)- or a (μ-hydroxo)(μ-carboxylato)diiron(III) core structure, respectively. The observation of these two different core structures, together with the crystallographic results of the MMOH from Methylococcus capsulatus (Bath), suggests the presence of an equilibrium that may reflect a core flexibility that is required to accommodate the various intermediates in the catalytic cycle of the enzyme. XAS studies on the binding of component B (MMOB) to the hydroxylase component show that MMOB does not perturb either this equilibrium or the gross structure of the oxidized diiron site in MMOH.Type of Medium: Electronic ResourceURL: