A stable electrode for high-potential, electrocatalytic O(2) reduction based on rational attachment of a blue copper oxidase to a graphite surface.
about
Rationally tuning the reduction potential of a single cupredoxin beyond the natural rangeCrystal structure of an ascomycete fungal laccase from Thielavia arenaria--common structural features of asco-laccasesBilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reductionStructural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidaseRational design of quinones for high power density biofuel cells.Mononuclear copper complex-catalyzed four-electron reduction of oxygen.Direct, Electrocatalytic Oxygen Reduction by Laccase on Anthracene-2-methanethiol Modified Gold.Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes.Direct electrochemistry of glucose oxidase on novel free-standing nitrogen-doped carbon nanospheres@carbon nanofibers composite film.Electron-transfer reduction of dinuclear copper peroxo and bis-μ-oxo complexes leading to the catalytic four-electron reduction of dioxygen to water.Lewis acid-induced change from four- to two-electron reduction of dioxygen catalyzed by copper complexes using scandium triflateA biosynthetic model of cytochrome c oxidase as an electrocatalyst for oxygen reduction.Temperature-independent catalytic two-electron reduction of dioxygen by ferrocenes with a copper(II) tris[2-(2-pyridyl)ethyl]amine catalyst in the presence of perchloric acid.Modified reactivity toward O2 in first shell variants of Fet3p: geometric and electronic structure requirements for a functioning trinuclear copper clusterEnzymes as modular catalysts for redox half-reactions in H2-powered chemical synthesis: from biology to technology.Electrografting: a powerful method for surface modification.Enzymatic versus microbial bio-catalyzed electrodes in bio-electrochemical systems.Integration of photoswitchable proteins, photosynthetic reaction centers and semiconductor/biomolecule hybrids with electrode supports for optobioelectronic applications.Cathodic catalysts in bioelectrochemical systems for energy recovery from wastewater.Reconstitution of supramolecular organization involved in energy metabolism at electrochemical interfaces for biosensing and bioenergy production.Recent progress in oxygen-reducing laccase biocathodes for enzymatic biofuel cells.Structure and Modification of Electrode Materials for Protein Electrochemistry.Direct enzymatic bioelectrocatalysis: differentiating between myth and reality.Prolongation of electrode lifetime in biofuel cells by periodic enzyme renewal.Covalent immobilization of oriented photosystem II on a nanostructured electrode for solar water oxidation.Catalysis of dioxygen reduction by Thermus thermophilus strain HB27 laccase on ketjen black electrodesCellobiose dehydrogenase aryl diazonium modified single walled carbon nanotubes: enhanced direct electron transfer through a positively charged surfaceSupramolecular immobilization of laccase on carbon nanotube electrodes functionalized with (methylpyrenylaminomethyl)anthraquinone for direct electron reduction of oxygen.Improvement of a direct electron transfer-type fructose/dioxygen biofuel cell with a substrate-modified biocathode.Prediction of Reduction Potentials of Copper Proteins with Continuum Electrostatics and Density Functional Theory.Bilirubin oxidase bioelectrocatalytic cathodes: the impact of hydrogen peroxide.Diazonium Functionalisation of Carbon Nanotubes for Specific Orientation of Multicopper Oxidases: Controlling Electron Entry Points and Oxygen Diffusion to the Enzyme.Effect of circular permutation on the structure and function of type 1 blue copper center in azurin.Electrocatalytic O2 Reduction at a Bio-inspired Mononuclear Copper Phenolato Complex Immobilized on a Carbon Nanotube Electrode.Bioinspired copper catalyst effective for both reduction and evolution of oxygen.Efficient electrocatalytic oxygen reduction by the 'blue' copper oxidase, laccase, directly attached to chemically modified carbons.Fully Oriented Bilirubin Oxidase on Porphyrin-Functionalized Carbon Nanotube Electrodes for Electrocatalytic Oxygen Reduction.Effect of enzymatic orientation through the use of syringaldazine molecules on multiple multi-copper oxidase enzymes.Methodologies for wiring redox proteins/enzymes to electrode surfaces.Wiring laccase on covalently modified graphene: carbon nanotube assemblies for the direct bio-electrocatalytic reduction of oxygen.
P2860
Q27658066-1944A773-FC3A-4CDE-9B64-30CE5EE7CC80Q27667644-D196A57D-470A-4CEE-91B3-1D82B9DDD534Q27667730-91D02B21-1A23-45F6-B9D2-8B5841EF4F8AQ27678685-BD784323-48BE-4241-B3BF-4841F74E5DF8Q33886469-1AC1FDD2-2CF9-4CB0-8BFE-069E88B593B0Q33915839-BD8E8973-6D04-4D24-BA7A-7915EF1FD9EAQ34121952-B0660621-247D-4325-AE04-C110B7B34019Q35180570-863A88EC-9B55-4952-9363-C5605ED65F0DQ35574835-16715A2E-0E6E-42B1-B182-E9BB7588619BQ35862346-CAD5057E-0847-4A74-89F2-41DE81E3CBAAQ36240088-D3432105-6139-43D7-91EF-719451EEBB45Q36249818-B2FB6278-BD0D-4843-A22A-FEB83579A64EQ36679841-D2119866-6FD0-4979-88CD-BBE8326727A7Q37257624-D77246BF-D73C-4620-93DD-1BFBD12F32A2Q37632855-1277733F-8B8F-4948-9FAC-A7FE705A6038Q37866649-EE0AFB57-5659-441A-BDB4-B72574AF74E8Q38016820-5E547A39-B7A4-4B47-93D5-D8E8256D1D41Q38039034-6D1D1B9A-7DAE-4AD0-AB2F-87DAAF1D8FA8Q38130129-89E09CF9-F131-45A5-9487-00A12CCFA111Q38167617-991AD5B0-375D-4BAE-837F-7A24EF8B884AQ38313750-BAA94931-ED85-4399-803C-3E4A5BB5A1E7Q38923180-D9F7DAB8-8FB5-41AA-84D2-DF6C98CEEF54Q39388973-F856E45A-3193-4FC9-B170-EF894267E535Q40062237-74B56742-1181-41DA-B9AB-6C9068A3C3C2Q41761087-E1BAD5E2-C875-4E27-97C2-D7DB2CA8EDB7Q42138560-3DE57577-87B0-4158-BC4A-77882B0D5E84Q42717018-0C485791-44A6-4295-9F06-6B9B4012128AQ43712812-B3D81980-8853-4A65-9DA7-749987F7D386Q45281853-99229969-845B-4235-A77B-1383F55CFBD3Q46244289-2D5EDD2C-97D3-490B-A4D4-D95F94A96096Q46786153-FB5ACB7B-AB8F-4BAC-BC91-7D6BA077CA84Q48191662-9E39015C-938A-45B9-9AF3-FA64D64BD02AQ48248286-A5B78108-A8D6-43BB-83A7-A88A34343D02Q48266012-0BE9439C-B69A-4D33-95AC-84428CA2B283Q50447297-EB32DAB5-DFA0-44C8-ADE6-AC7459B2ED29Q50454282-D32F0D92-F07D-4E7E-83D4-654D99F40856Q51693063-096E2B1D-0219-4310-AB90-67B47757E344Q51720848-0C1C2D46-34BE-415B-A91D-9E936F1CC1F8Q52594680-6F874857-479E-43EB-ACA7-4A2620D0B1F5Q53361312-43FB1A7C-060F-4CAE-A525-56D8FAB6A458
P2860
A stable electrode for high-potential, electrocatalytic O(2) reduction based on rational attachment of a blue copper oxidase to a graphite surface.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
A stable electrode for high-po ...... oxidase to a graphite surface.
@en
A stable electrode for high-po ...... oxidase to a graphite surface.
@nl
type
label
A stable electrode for high-po ...... oxidase to a graphite surface.
@en
A stable electrode for high-po ...... oxidase to a graphite surface.
@nl
prefLabel
A stable electrode for high-po ...... oxidase to a graphite surface.
@en
A stable electrode for high-po ...... oxidase to a graphite surface.
@nl
P356
P1476
A stable electrode for high-po ...... oxidase to a graphite surface.
@en
P2093
Fraser A Armstrong
Rachel S Heath
P304
P356
10.1039/B703114A
P407
P577
2007-04-03T00:00:00Z