Search Results - "Hagen, W R"

Ferritin-supported palladium nanoclusters: selective catalysts for aerobic oxidations in water by Kanbak-Aksu, S, Nahid Hasan, M, Hagen, W R, Hollmann, F, Sordi, D, Sheldon, R A, Arends, I W C E

“…Confinement of nanometallic Pd within the core of a hyperthermophilic ferritin cage (from Pyrococcus furiosus) is reported. The resulting nanostructured hybrid…”
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Density Functional Calculations of g-Tensors of Low-Spin Iron(I) and Iron(III) Porphyrins by van Lenthe, E, van der Avoird, A, Hagen, W. R, Reijerse, E. J

“…The g-values of some selected low-spin Fe(I) and Fe(III) porphyrin complexes have been calculated, using a method based on density functional theory and the…”
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Hybrid-Cluster Protein (HCP) from Desulfovibrio vulgaris (Hildenborough) at 1.6 Å Resolution by Cooper, S. J, Garner, C. D, Hagen, W. R, Lindley, P. F, Bailey, S

“…The three-dimensional structure of the hybrid cluster protein from Desulfovibrio vulgaris (Hildenborough) has been determined at 1.6 Å resolution using…”
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Direct hydride transfer in the reaction mechanism of quinoprotein alcohol dehydrogenases: a quantum mechanical investigation by Jongejan, A., Jongejan, J. A., Hagen, W. R.

“…Oxidation of alcohols by direct hydride transfer to the pyrroloquinoline quinone (PQQ) cofactor of quinoprotein alcohol dehydrogenases has been studied using…”
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On the relationship between affinity for molecular hydrogen and the physiological directionality of hydrogenases by van Haaster, D J, Hagedoorn, P-L, Jongejan, J A, Hagen, W R

“…The physiological significance of the generic reaction H(2)<-->2[H] is not always clear because hydrogenases may function in the breakdown of molecular…”
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Influence of Charge and Polarity on the Redox Potentials of High-Potential Iron-Sulfur Proteins: Evidence for the Existence of Two Groups by Heering, H. A, Bulsink, Y. B. M, Hagen, W. R, Meyer, T. E

“…We have investigated the HiPIPs from Ectothiorhodospira vacuolata (iso-1 and iso-2), Chromatium vinosum, Rhodocyclus gelatinosus, Rhodocyclus tenuis (strain…”
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Pyrococcus furiosus ferredoxin is a functional dimer by Hasan, M.N, Hagedoorn, P.L, Hagen, W.R

“…Pyrococcus furiosus ferredoxin is subject to a monomer/dimer equilibrium as a function of ionic strength. At physiological ionic strength, approximately 0.35 M…”
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Overproduction, purification and novel redox properties of the dihaem cytochrome c, NapB, from Haemophilus influenzae by Brigé, A, Cole, J A, Hagen, W R, Guisez, Y, Van Beeumen, J J

“…The napB gene of the pathogenic bacterium Haemophilus influenzae encodes a dihaem cytochrome c, the small subunit of a heterodimeric periplasmic nitrate…”
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Purification and characterization of a benzylviologen-linked, tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas by Hensgens, C M, Hagen, W R, Hansen, T A

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On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus: topology, structure, and temperature-dependent redox chemistry by Silva, P J, de Castro, B, Hagen, W R

“…The sulfhydrogenase complex of Pyrococcus furiosus is an alpha beta gamma delta heterotetramer with both hydrogenase activity (borne by the alpha delta…”
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Characterization of the Corrinoid Iron-Sulfur Protein Tetrachloroethene Reductive Dehalogenase of Dehalobacter restrictus by MAILLARD, Julien, SCHUMACHER, Wolfram, VAZQUEZ, Francisco, REGEARD, Christophe, HAGEN, Wilfred R, HOLLIGER, Christof

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Complex electrochemistry of flavodoxin at carbon-based electrodes: results from a combination of direct electron transfer, flavin-mediated electron transfer and comproportionation by Heering, H.A., Hagen, W.R.

“…Staircase cyclic voltammetry (SCV) and differential pulse voltammetry on fully oxidized flavodoxin from Desulfovibrio vulgaris Hildenborough at the bare glassy…”
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Redox properties and electron paramagnetic resonance spectroscopy of the transition state complex of Azotobacter vinelandii nitrogenase by Spee, J.H., Arendsen, A.F., Wassink, H., Marritt, S.J., Hagen, W.R., Haaker, H.

“…Nitrogenase is a two-component metalloenzyme that catalyzes a MgATP hydrolysis driven reduction of substrates. Aluminum fluoride plus MgADP inhibits…”
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Spectroscopic studies on the iron-sulfur centers of milk xanthine oxidase by Hille, R, Hagen, W R, Dunham, W R

“…The optical electron paramagnetic resonance and Mössbauer spectral properties of the two iron-sulfur centers present in milk xanthine oxidase have been…”
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Estimation of higher-order magnetic spin interactions of Fe(III) and Gd(III) ions doped in α-alumina powder with multifrequency EPR by Priem, A., van Bentum, P. J. M., Hagen, W. R., Reijerse, E. J.

“…Fe(III) and Gd(III) ions in α-alumina (A12O3) exhibit spin states ofS = 5/2 andS = 7/2 respectively. The magnitude of the zero-field interaction (ZFI) (D =…”
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On the iron–sulfur clusters in the complex redox enzyme dihydropyrimidine dehydrogenase by Hagen, W. R., Vanoni, M. A., Rosenbaum, K., Schnackerz, K. D.

“…Porcine liver dihydropyrimidine dehydrogenase is a homodimeric iron–sulfur flavoenzyme that catalyses the first and rate‐limiting step of pyrimidine…”
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EPR spectroscopic characterization of an ‘iron only⌉ nitrogenase S = 3/2 spectrum of component 1 isolated from Rhodobacter capsulatus by Müller, Achim, Schneider, Klaus, Knüttel, Karlheinz, Hagen, Wilfred R.

“…The alternative nitrogenase of Rhodobacter capsulatus, isolated from a nifHDK deletion mutant, has been purified to near homogeneity and identified as an ‘iron…”
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Purification and Characterization of (Per)Chlorate Reductase from the Chlorate-Respiring Strain GR-1 by Kengen, S W, Rikken, G B, Hagen, W R, van Ginkel, C G, Stams, A J

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Direct electron transfer of redox proteins at the bare glassy carbon electrode by HAGEN, Wilfred R.

“…A simple system is presented for the microscale, direct voltammetry of redox proteins, typically 25 μg, in the absence of mediators and/or modifiers. The…”
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High-frequency EPR of transition ion complexes and metalloproteins by Hagen, Wilfred R.

“…For more than 50 years EPR spectoscopists have worked predominantly with the standard X-band microwave frequency of 9–10 GHz. Technical developments now make…”
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