Search Results - "Stiefel, E. I"

Overexpression and Characterization of an Iron Storage and DNA-Binding Dps Protein from Trichodesmium erythraeum by CASTRUITA, M, SAITO, M, SCHOTTEL, P. C, ELMEGREEN, L. A, MYNENI, S, STIEFEL, E. I, MOREL, F. M. M

“…Classifications Services AEM Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit…”
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Toward Separation and Purification of Olefins Using Dithiolene Complexes: An Electrochemical Approach by Wang, Kun, Stiefel, Edward I.

“…The complex Ni[S2C 2(CF3)2]2reacts with light olefins, including ethylene and propylene, selectively and reversibly. The reaction is not poisoned by hydrogen…”
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Nickel L-Edge Soft X-ray Spectroscopy of Nickel−Iron Hydrogenases and Model CompoundsEvidence for High-Spin Nickel(II) in the Active Enzyme by Wang, Hongxin, Ralston, C. Y, Patil, D. S, Jones, R. M, Gu, W, Verhagen, M, Adams, M, Ge, P, Riordan, C, Marganian, C. A, Mascharak, P, Kovacs, J, Miller, C. G, Collins, T. J, Brooker, S, Croucher, P. D, Wang, Kun, Stiefel, E. I, Cramer, S. P

“…L-edge X-ray absorption spectroscopy has been used to study, under a variety of conditions, the electronic structure of Ni in the Ni−Fe hydrogenases from…”
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Ligand and Tetrathiometalate Effects in Induced Internal Electron Transfer Reactions by McConnachie, C. A, Stiefel, E. I

“…New rhenium sulfide complexes, [ReIV 2(μ-S)2(μ-S2)(μ-S2COR)(S2COR)2]- and [ReIV 2(μ-S)2(S2COR)4], and a new tungsten sulfide complex, [WS(S2)(S2CC6H5)2], have…”
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Molybdenum Bolsters the Bioinorganic Brigade by Stiefel, Edward I.

“…The crystal structure of the simplest known molybdenum-requiring enzyme, the dimethyl sulfoxide reductase of Rhodobacter sphaeroides , is reported on in this…”
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A New Sulfur-Rich Rhenium(III) Complex, Re(S2CC6H5)(S3CC6H5)2, and Seven-Coordinate Complexes Formed by Reversible Sulfur Abstraction Reactions, Re(S2CC6H5)3(PPh3) and [Re(S2CC6H5)3(CN)] by McConnachie, C. A, Stiefel, E. I

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Unification of the Ferritin Family of Proteins by Grossman, M. J., Hinton, S. M., Minak-Bernero, V., Slaughter, C., Stiefel, E. I.

“…Ferritin is the iron-storage protein of eukaryotic organisms. The nucleotide sequence encoding Azotobacter vinelandii bacterioferritin, a hemoprotein, was…”
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Biological Hydrogen Production: Not so Elementary by Michael W. W. Adams, Stiefel, Edward I.

“…Hydrogenase is the family of enzymes that catalyze the interconversion of the smallest molecule, hydrogen gas. Researchers have used x-ray crystallography to…”
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Resonance Raman Spectroscopic Characterization of the Molybdopterin Active Site of DMSO Reductase by Kilpatrick, L, Rajagopalan, K. V, Hilton, J, Bastian, N. R, Stiefel, E. I, Pilato, R. S, Spiro, T. G

“…Resonance Raman spectra are compared for Rhodobacter sphaeroides dimethyl sulfoxide reductase, an enzyme containing a molybdopterin cofactor, and two model…”
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Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes by Stiefel, E. I.

“…Abstract…”
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Synthesis and characterization of mononuclear and dinuclear bis(2,2'-bipyridine)ruthenium(II) complexes containing sulfur-donor ligands by Greaney, M. A, Coyle, C. L, Harmer, M. A, Jordan, A, Stiefel, E. I

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Redox properties and Mossbauer spectroscopy of Azotobacter vinelandii bacterioferritin by Watt, G.D, Frankel, R.B, Papaefthymiou, G.C, Spartalian, K, Stiefel, E.I

“…Biochemical characterization, redox measurements, and Moessbauer spectral data of reduced and oxidized bacterial ferritin from Azotobacter vinelandii are…”
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Organometallic iron: the key to biological hydrogen metabolism by Adams, Michael WW, Stiefel, Edward I

“…X-ray crystallography of iron-hydrogenases reveals that the active-site H-cluster contains an unmistakably organometallic dinuclear iron subcluster. The…”
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Direct observation of bis-sulfur ligation to the heme of bacterioferritin by George, Graham N, Richards, Thomas, Bare, Richard E, Gea, Yeunjong, Prince, Roger C, Stiefel, Edward I, Watt, Gerald D

“…X-ray absorption spectroscopy was used to examine the ligation of the heme of Azobacter vinelandii bacterioferritin scrupulously cleaned of non-heme iron. We…”
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Iron-molybdenum cofactor from nitrogenase. Modified extraction methods as probes for composition by Yang, S S, Pan, W H, Friesen, G D, Burgess, B K, Corbin, J L, Stiefel, E I, Newton, W E

“…Five modifications of the preparative procedure for isolating iron-molybdenum cofactor (FeMoco) from the molybdenum-iron (MoFe) protein of Azotobacter…”
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Protein nitrogen coordination to the FeMo center of nitrogenase from Clostridium Pasteurianum by THOMANN, H, MORGAN, T. V, JIN, H, BURGMAYER, S. J. N, BARE, R. E, STIEFEL, E. I

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Synthesis, structure, and reactivity of [(C2H5)4N]2[Mo3(μ3-S)(μ2-S)3(SCH2CH2S)3]: a cluster with sulfur vacancies and resonance Raman spectral similarity to Fe3S4 proteins by HALBERT, T. R, MCGAULEY, K, PAN, W.-H, CZERNUSZEWICZ, R. S, STIEFEL, E. I

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Oxidation-reduction properties and complexation reactions of the iron-molybdenum cofactor of nitrogenase by Burgess, B K, Stiefel, E I, Newton, W E

“…The interactions of the iron-molybdenum cofactor, FeMoco, isolated from acid-treated Azotobacter vinelandii molybdenum-iron protein (Av1) with EDTA and…”
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Bacterioferritin: a hemoprotein member of the ferritin family by Stiefel, E I, Grossman, M J, Hinton, S M, Minak-Bernero, V, George, G N, Prince, R C, Bare, R E, Watt, G D

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Large-scale purification of high activity Azotobacter vinelandII nitrogenase by Burgess, B K, Jacobs, D B, Stiefel, E I

“…A large scale, rapid, high-yield purification procedure for Azotobacter vinelandii nitrogenase proteins has been developed. Yields of approx. 600 mg of the…”
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