about
Docking and migration of carbon monoxide in nitrogenase: the case for gated pockets from infrared spectroscopy and molecular dynamicsHydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopyReversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenaseA theoretical study of the mechanism for peptide hydrolysis by thermolysinLow frequency dynamics of the nitrogenase MoFe protein via femtosecond pump probe spectroscopy - Observation of a candidate promoting vibrationCharacterization of the [3Fe-4S](0/1+) cluster from the D14C variant of Pyrococcus furiosus ferredoxin via combined NRVS and DFT analyses.Dynamics of the [4Fe-4S] cluster in Pyrococcus furiosus D14C ferredoxin via nuclear resonance vibrational and resonance Raman spectroscopies, force field simulations, and density functional theory calculations.Characterization of the Fe site in iron-sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS).Synthesis and vibrational spectroscopy of (57)Fe-labeled models of [NiFe] hydrogenase: first direct observation of a nickel-iron interactionStructural characterization of CO-inhibited Mo-nitrogenase by combined application of nuclear resonance vibrational spectroscopy, extended X-ray absorption fine structure, and density functional theory: new insights into the effects of CO binding anNickel superoxide dismutase reaction mechanism studied by hybrid density functional methods.Fe-H/D stretching and bending modes in nuclear resonant vibrational, Raman and infrared spectroscopies: comparisons of density functional theory and experiment.IR-monitored photolysis of CO-inhibited nitrogenase: a major EPR-silent species with coupled terminal CO ligandsThe HydG enzyme generates an Fe(CO)2(CN) synthon in assembly of the FeFe hydrogenase H-cluster.The Mössbauer Parameters of the Proximal Cluster of Membrane-Bound Hydrogenase Revisited: A Density Functional Theory StudyCharacterization of [4Fe-4S] cluster vibrations and structure in nitrogenase Fe protein at three oxidation levels via combined NRVS, EXAFS, and DFT analysesLigand-bound S = 1/2 FeMo-cofactor of nitrogenase: hyperfine interaction analysis and implication for the central ligand X identity.Catalysis by methyl-coenzyme M reductase: a theoretical study for heterodisulfide product formation.Class I ribonucleotide reductase revisited: the effect of removing a proton on Glu441.Direct Observation of an Iron-Bound Terminal Hydride in [FeFe]-Hydrogenase by Nuclear Resonance Vibrational Spectroscopy.Reaction Coordinate Leading to H2 Production in [FeFe]-Hydrogenase Identified by Nuclear Resonance Vibrational Spectroscopy and Density Functional Theory.Copper-zinc superoxide dismutase: theoretical insights into the catalytic mechanism.Testing if the interstitial atom, X, of the nitrogenase molybdenum-iron cofactor is N or C: ENDOR, ESEEM, and DFT studies of the S = 3/2 resting state in multiple environments.Redox-dependent structural transformations of the [4Fe-3S] proximal cluster in O2-tolerant membrane-bound [NiFe]-hydrogenase: a DFT study.Sterically Stabilized Terminal Hydride of a Diiron Dithiolate.Resonance Raman Spectroscopic Analysis of the [NiFe] Active Site and the Proximal [4Fe-3S] Cluster of an O2-Tolerant Membrane-Bound Hydrogenase in the Crystalline StateA mechanism from quantum chemical studies for methane formation in methanogenesisIs there a Ni-methyl intermediate in the mechanism of methyl-coenzyme M reductase?High-Frequency Fe-H Vibrations in a Bridging Hydride Complex Characterized by NRVS and DFTTerminal Hydride Species in [FeFe]-Hydrogenases Are Vibrationally Coupled to the Active Site EnvironmentAsymmetry in the Ligand Coordination Sphere of the [FeFe] Hydrogenase Active Site Is Reflected in the Magnetic Spin Interactions of the Aza-propanedithiolate LigandInsights from 125Te and 57Fe nuclear resonance vibrational spectroscopy: a [4Fe-4Te] cluster from two points of viewSpectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates
P50
Q27301771-1F1FAA81-6A6F-403F-92E3-A651576CB721Q27323823-C3D19A11-9D64-40C9-AD2D-9811FB781DEDQ27690017-D775473A-8EF7-409D-90E5-438B6EE8CD6DQ28213187-E3777AF7-05A8-4913-BC7C-5320B350B45DQ28600846-4EC097DA-C3FB-462E-B8BD-FD5068C5C82AQ30358107-DEA9531B-BF7D-4475-BB02-1E626A44D43FQ30466601-DFC55F73-0448-466D-912D-1F9B967BF36BQ30487338-9EBA2EB6-5DF3-4CBF-9C1E-5B2C1AC786BCQ34315305-B23E6145-0BE1-40AA-AAE2-C34AB0F49057Q34531428-A0B1241A-67FF-4E37-832D-C71752B37E5DQ34535069-49BD1BEA-3C87-469F-873D-D498D7BD48D8Q34681898-1227ABFA-0999-4EA3-9E37-EDF74680CBEBQ35835570-4A40C189-898D-4439-B084-D01E0E990FAAQ35886414-4ABF6211-6E4A-4FB5-9016-66593860660AQ36762382-7B5C9713-E96E-4FDC-8BB9-D039CE2430A8Q36816897-79390ECB-060F-4919-A728-D96B7F4BA661Q42529551-A737519A-A933-45E1-8AE4-3E05240AB3C3Q44427736-73DF85AF-FA1E-45E9-94E8-791C27413575Q44706656-88464D1E-402B-4A18-AF0F-7CB12BE738BDQ46404435-DFF71038-A36B-48B9-867F-898A6B74C815Q46451346-2FF5B926-9C90-4E6E-8314-9355CE275EB5Q46451444-30199DA6-1E3C-4084-BE41-E708419BDCFFQ46890112-DCD999A2-C47B-48E7-AA6F-B908DC0AEB48Q48019723-29DBEC4D-4E9A-4C3A-938C-FFAEB5556C3FQ48135195-9AD9F1B0-835F-407D-8C22-9E20095CF5EFQ56990005-95BB4ACC-307B-4B8E-BFF4-5A2600C8CEB3Q77907009-B3AE0C19-4600-46B7-8B4B-782BBE1B3560Q84151962-5E1895F9-906B-4F7B-BCB9-9176000A0CCBQ88920631-F3D025A9-B7A1-48DB-8951-80E2A1D653B4Q89162648-9A3589DC-21FC-40F8-AF9B-B06F2FB92D5AQ90455368-74EA01C7-18A2-4BA9-9C1E-B9FE6C6042D6Q90534763-7C6A81F4-1D09-4D32-88DF-7CCC6EC7872DQ91840369-9179A355-F992-45D5-96EC-D78C4CF6F453
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Vladimir Pelmenschikov
@ast
Vladimir Pelmenschikov
@en
Vladimir Pelmenschikov
@es
Vladimir Pelmenschikov
@nl
Vladimir Pelmenschikov
@sl
type
label
Vladimir Pelmenschikov
@ast
Vladimir Pelmenschikov
@en
Vladimir Pelmenschikov
@es
Vladimir Pelmenschikov
@nl
Vladimir Pelmenschikov
@sl
prefLabel
Vladimir Pelmenschikov
@ast
Vladimir Pelmenschikov
@en
Vladimir Pelmenschikov
@es
Vladimir Pelmenschikov
@nl
Vladimir Pelmenschikov
@sl
P106
P21
P31
P496
0000-0002-0523-4418