about
Dithiomethylether as a ligand in the hydrogenase h-clusterTheoretical studies of biological nitrogen fixation. I. Density functional modeling of the Mo-site of the FeMo-cofactor.In silico evaluation of proposed biosynthetic pathways for the unique dithiolate ligand of the H-cluster of [FeFe]-hydrogenase.Electronic structural investigations of ruthenium compounds and anticancer prodrugs.Combined Mössbauer spectroscopic, multi-edge X-ray absorption spectroscopic, and density functional theoretical study of the radical SAM enzyme spore photoproduct lyase.Sulfur K-edge X-ray absorption spectroscopy as a probe of ligand-metal bond covalency: metal vs ligand oxidation in copper and nickel dithiolene complexesSulfur K-edge X-ray absorption spectroscopy and density functional calculations on Mo(IV) and Mo(VI)=O bis-dithiolenes: insights into the mechanism of oxo transfer in DMSO reductase and related functional analoguesSulfur K-edge XAS of WVO vs. MoVO bis(dithiolene) complexes: contributions of relativistic effects to electronic structure and reactivity of tungsten enzymes.S K-edge X-ray absorption spectroscopic investigation of the Ni-containing superoxide dismutase active site: new structural insight into the mechanism.Exploring new frontiers of nitrogenase structure and mechanism.Electronic structure and its relation to function in copper proteins.Comparative assessment of the composition and charge state of nitrogenase FeMo-cofactor.Production of a biomimetic Fe(I)-S phase on pyrite by atomic hydrogen beam surface reactive scattering.Three-coordinate copper(I) amido and aminyl radical complexesElectronic structures of metal sites in proteins and models: contributions to function in blue copper proteins.Probing the MgATP-bound conformation of the nitrogenase Fe protein by solution small-angle X-ray scattering.A radical solution for the biosynthesis of the H-cluster of hydrogenase.A mononuclear Fe(III) single molecule magnet with a 3/2↔5/2 spin crossover.Electronic control of the "Bailar twist" in formally d0-d2 molybdenum tris(dithiolene) complexes: a sulfur K-edge X-ray absorption spectroscopy and density functional theory study.Nitrogenase structure and function relationships by density functional theory.A novel 1,3,5-triaminocyclohexane-based tripodal ligand forms a unique tetra(pyrazolate)-bridged tricopper(ii) core: solution equilibrium, structure and catecholase activity.Mono- and binuclear tris(3-tert-butyl-2-sulfanylidene-1H-imidazol-1-yl)hydroborate bismuth(III) dichloride complexes: a soft scorpionate ligand can coordinate to p-block elements.Role of the Tyr-Cys cross-link to the active site properties of galactose oxidase.Probing the electronic structures of [Cu2(mu-XR2)]n+ diamond cores as a function of the bridging X atom (X = N or P) and charge (n = 0, 1, 2).Spectroscopic characterization of the Leu513His variant of fungal laccase: effect of increased axial ligand interaction on the geometric and electronic structure of the type 1 Cu site.Spectroscopic studies of the Met182Thr mutant of nitrite reductase: role of the axial ligand in the geometric and electronic structure of blue and green copper sites.Description of the ground state wave functions of Ni dithiolenes using sulfur K-edge X-ray absorption spectroscopy.Multi-edge X-ray absorption spectroscopy. 1. X-ray absorption near-edge structure analysis of a biomimetic model of FeFe-hydrogenase.Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.The solution structure of [Cu(aq)]2+ and its implications for rack-induced bonding in blue copper protein active sites.Spectroscopic investigation of stellacyanin mutants: axial ligand interactions at the blue copper site.Multiedge X-ray Absorption Spectroscopy Part II: XANES Analysis of Bridging and Terminal Chlorides in Hexachlorodipalladate(II) Complex.Sulfur K-edge X-ray absorption spectroscopy as an experimental probe for S-nitroso proteins.Spin-Polarization-Induced Preedge Transitions in the Sulfur K-Edge XAS Spectra of Open-Shell Transition-Metal Sulfates: Spectroscopic Validation of σ-Bond Electron Transfer.Electronic structure of transition metal-cysteine complexes from X-ray absorption spectroscopy.Influence of ligand flexibility on the electronic structure of oxidized Ni(III)-phenoxide complexes.Systematic development of computational models for the catalytic site in galactose oxidase: impact of outer-sphere residues on the geometric and electronic structures.Reduction of nitrite and nitrate to ammonium on pyrite.Surface Characterization of Mechanochemically Modified Exfoliated Halloysite Nanoscrolls.A quantitative description of the ground-state wave function of Cu(A) by X-ray absorption spectroscopy: comparison to plastocyanin and relevance to electron transfer.
P50
Q27650022-68B0B85E-05B7-4801-B7B7-7024C5F06F71Q32064378-BC3DB544-788D-4E21-8CE8-040C47CB0424Q33352221-080CC79E-040E-40DF-B00D-7F3142B81A35Q33427427-F7E7793A-EB49-4BB5-A490-9EF99EB825D5Q33873928-6FA5B16B-EA29-4DB4-8F17-6CB0417279CEQ33891978-486901A9-91C3-4163-B137-1B1F9ECF2D4BQ34007410-39FB20C3-C73D-4C5F-A2BF-E333393C09EDQ34133196-11763904-4628-47A8-9EA1-4A6507008C45Q34304404-D79F8DD2-7D56-499F-960E-AECD2F43F2EAQ34498629-B602F980-7D10-43F0-B224-39B04F740CFCQ34662144-A46F2179-3A51-48DF-B98A-2FA3AB210DE2Q35017261-B079592C-3FC8-4D9A-8FB1-2EADE3A448EEQ35033366-09E346A9-E658-4C1C-995D-1111584556D5Q35033373-D8C4AAFD-4832-4D86-9959-82DCE79BA50AQ35660851-0D3D9E54-2900-4AF9-800C-BD27825715EBQ35789254-65736E88-997F-4A48-A62E-0E05F6551130Q36357090-2A22BE8E-1933-417D-8570-A4532D220852Q36390640-064812CD-F47A-4EBD-AD90-FA08652CDB23Q37037844-9ED73E33-358E-4A92-8514-B2D7FC558961Q37915419-E0FD622E-C297-4345-87EA-6396BE8F2430Q39454947-28E82D90-87E3-456A-9E0F-1BFAF3EB2B1AQ42733622-4D7E9558-A346-4F0B-8AF6-98CACC84D612Q43413056-6A626CB8-55CF-4A11-9E0D-4D6C0F9F7B07Q44247577-DD6E591D-B623-480C-8624-0CC2BA0E3F69Q44485118-6EEDFBC1-8729-45C8-84C5-7C6E43E86055Q44670321-1F301E17-9A03-4CC8-ADA4-41B9428A5DFEQ45060178-9AFD9D16-B803-4750-80F8-D656B36F40E7Q45064737-B191A0DA-B68C-4076-AC7B-98048169A077Q45925557-CD4A44F9-216E-4967-8F4E-D312ACE6590FQ46007009-6A219A1D-50BB-4099-ABDA-D5E119ABAF09Q46062554-5BC68B32-5AC1-4EBA-A6A5-E86A4BAA0969Q46259744-CC20F768-85D8-46CA-9335-DCAA1F1C2ED8Q46395112-79A5A9D0-D305-4F14-9DDB-33989A1C8B4BQ46617381-F570B896-03BD-455A-B804-862C2245C6EAQ46693130-98CE44B2-D9CF-4C11-A883-4588C6DA2DB2Q46834109-98F73A08-3071-4F51-96A5-FAD698E1AD99Q46867308-59D87D5D-1722-441F-9C83-F8FC5E2DDE05Q47802338-6E96EB7D-83F5-47AE-9951-A66928C160E0Q48045140-8199724C-6D21-4C2C-BCBA-F829ED57DDF7Q50505030-74EE0706-E9EE-4E08-A405-83A5DC82D7AF
P50
description
hulumtues
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researcher
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հետազոտող
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name
Robert K. Szilagyi
@ast
Robert K. Szilagyi
@en
Robert K. Szilagyi
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Robert K. Szilagyi
@nl
Robert K. Szilagyi
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type
label
Robert K. Szilagyi
@ast
Robert K. Szilagyi
@en
Robert K. Szilagyi
@es
Robert K. Szilagyi
@nl
Robert K. Szilagyi
@sl
prefLabel
Robert K. Szilagyi
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Robert K. Szilagyi
@en
Robert K. Szilagyi
@es
Robert K. Szilagyi
@nl
Robert K. Szilagyi
@sl
P1053
G-9268-2012
P106
P1153
6701693729
P21
P2456
P31
P3829
P496
0000-0002-9314-6222