about
Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenasesThe Copper Active Site of CBM33 Polysaccharide OxygenasesX-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coliHow the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenaseCrystal structure of the O(2)-tolerant membrane-bound hydrogenase 1 from Escherichia coli in complex with its cognate cytochrome bUnderstanding and Harnessing Hydrogenases, Biological Dihydrogen CatalystsThe electrophotonic silicon biosensorAnalysis of HypD Disulfide Redox Chemistry via Optimization of Fourier Transformed ac Voltammetric Data.Electrochemical evidence that pyranopterin redox chemistry controls the catalysis of YedY, a mononuclear Mo enzyme.Integration of an [FeFe]-hydrogenase into the anaerobic metabolism of Escherichia coli.Investigating and exploiting the electrocatalytic properties of hydrogenases.Dynamic electrochemical investigations of hydrogen oxidation and production by enzymes and implications for future technology.The hows and whys of aerobic H2 metabolism.Probing biological redox chemistry with large amplitude Fourier transformed ac voltammetry.Hydrogen cycling by enzymes: electrocatalysis and implications for future energy technology.Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.Water-gas shift reaction catalyzed by redox enzymes on conducting graphite platelets.Rapid and efficient electrocatalytic CO2/CO interconversions by Carboxydothermus hydrogenoformans CO dehydrogenase I on an electrode.How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.Structural differences of oxidized iron-sulfur and nickel-iron cofactors in O2-tolerant and O2-sensitive hydrogenases studied by X-ray absorption spectroscopy.Oxygen-tolerant [NiFe]-hydrogenases: the individual and collective importance of supernumerary cysteines at the proximal Fe-S cluster.Theoretical analysis of the two-electron transfer reaction and experimental studies with surface-confined cytochrome c peroxidase using large-amplitude Fourier transformed AC voltammetry.Capacitance-Assisted Sustainable Electrochemical Carbon Dioxide Mineralisation.Redox-Tagged Carbon Monoxide-Releasing Molecules (CORMs): Ferrocene-Containing [Mn(C^N)(CO)4] Complexes as a Promising New CORM Class.Biosynthesis of Salmonella enterica [NiFe]-hydrogenase-5: probing the roles of system-specific accessory proteins.How Salmonella oxidises H(2) under aerobic conditions.The Antimicrobial Activity of a Carbon Monoxide Releasing Molecule (EBOR-CORM-1) Is Shaped by Intraspecific Variation within Pseudomonas aeruginosa Populations.Methodologies for wiring redox proteins/enzymes to electrode surfaces.Principles of sustained enzymatic hydrogen oxidation in the presence of oxygen--the crucial influence of high potential Fe-S clusters in the electron relay of [NiFe]-hydrogenases.The difference a Se makes? Oxygen-tolerant hydrogen production by the [NiFeSe]-hydrogenase from Desulfomicrobium baculatum.Electrochemical investigations of the interconversions between catalytic and inhibited states of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans.Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases.Selective Extraction and In Situ Reduction of Precious Metal Salts from Model Waste To Generate Hybrid Gels with Embedded Electrocatalytic Nanoparticles.Conserved Histidine Adjacent to the Proximal Cluster Tunes the Anaerobic Reductive Activation of Escherichia coli Membrane-Bound [NiFe] Hydrogenase-1.Theoretical and experimental investigation of surface-confined two-center metalloproteins by large-amplitude Fourier transformed ac voltammetryCover Feature: Capacitance-Assisted Sustainable Electrochemical Carbon Dioxide Mineralisation (ChemSusChem 1/2018)Exploring the scope of capacitance-assisted electrochemical carbon dioxide captureFrontispiece: Methodologies for “Wiring” Redox Proteins/Enzymes to Electrode SurfacesX-ray structural, functional and computational studies of the O2-sensitive E. coli hydrogenase-1 C19G variant reveal an unusual [4Fe–4S] cluster
P50
Q26767154-B0894913-0142-45D4-8B8F-44493F827719Q27677120-D73F59B1-9D9C-4309-ACD8-EA6A9867F0E6Q27678099-C7F9FE10-4DED-4E5F-9134-F56C44A40CC3Q27681350-F44341CC-BA5C-4A69-91BE-BADAFDF93325Q27683625-7E85302B-FB4C-4BB8-88D0-F5E9C93FBF9EQ28109407-F739E6FA-DAD2-4727-9EF8-D98249CF87C9Q28829952-2D14B885-F9C4-461E-AC35-4F968AAD9040Q30313582-6561BE83-A989-4B57-95D8-A89E120BE3B0Q36331923-E9206F67-FC43-4861-BA86-854968E7952EQ36412465-5B0EF3A2-970D-496F-B521-80A5E42BEC28Q36936294-8D2AB6D0-EFB4-4A4F-B7EC-2B0474922F69Q37352673-29645D3E-48E9-41C3-B0BC-15648C4B5C50Q37988269-E4A85C6A-C422-4E2F-B98C-2ED637EF99E3Q38626511-68BE94A8-F46B-4340-A2E6-31730C141468Q40380031-2B6D6751-4CA5-4255-9270-93BA5F4330F7Q41206125-5730FFAF-FC1D-40A0-B4BC-4483D0080709Q41456603-4F2CD12B-6A6D-4B53-B7E2-20A85799DF37Q41860979-0952C68B-9181-4041-973C-61DAD6802FCDQ42683526-79E17B4F-3973-42B6-B5E8-600DF89F1906Q42913850-BD7F1A98-C52D-4C9E-ABD9-491B2C2E1B69Q44175539-AD688E2B-44DD-4EA4-A986-7F8C44DF506EQ45733027-83FE4B79-2C7D-42B0-B9C3-1AF2800D188CQ47745213-A083B72B-F8D4-429D-9251-1366F254CECFQ48048130-68542197-AE51-43AF-837E-6C77721FD495Q48258874-FE2B5553-A06B-452A-95C0-FBA5FF4E1D17Q49962308-9A02D459-245C-4542-9C2A-EAB6CF97E387Q50038757-EEE0D842-41BD-4FD7-A5C8-1EFD16742342Q51748626-9E997758-E467-456B-AF2A-7CFFC494E951Q52594680-9EEC6115-17C4-4942-8B00-29F96A62229AQ53341627-4093955C-AECB-4464-933C-F7C350F881BEQ53530323-32555ADC-3284-47E7-AA84-4F3F60B74339Q53582452-155C3441-41A2-4B5F-8260-AE342954395BQ53607575-EDC3D99F-C3B5-483D-A64F-69CE800D209FQ53657352-B245F264-184C-402D-92D2-6B50A7258EC3Q55154331-A27EF58D-CF00-4BD3-B834-5DA4B9D873C8Q57014612-B1FB1FE6-000D-4461-880A-D78DA90312F6Q59867776-97A5935C-86BB-4E58-A491-3D0FCF090B35Q59867800-E1898C9B-AB29-4FB1-A16F-F4542A8F626BQ60307423-A5B9BC70-F4A5-4508-AC91-4678549BAB13Q60307451-1094A5C6-B2E7-4A9E-A84C-602F404515BB
P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Alison Parkin
@ast
Alison Parkin
@en
Alison Parkin
@es
Alison Parkin
@nl
type
label
Alison Parkin
@ast
Alison Parkin
@en
Alison Parkin
@es
Alison Parkin
@nl
prefLabel
Alison Parkin
@ast
Alison Parkin
@en
Alison Parkin
@es
Alison Parkin
@nl
P1053
E-4508-2011
P106
P1153
10739528200
P2031
2005-01-01T00:00:00Z
P21
P31
P3829
P496
0000-0003-4715-7200
P569
2000-01-01T00:00:00Z