How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
about
Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenasesInvestigations of the efficient electrocatalytic interconversions of carbon dioxide and carbon monoxide by nickel-containing carbon monoxide dehydrogenasesNovel insights into the bioenergetics of mixed-acid fermentation: can hydrogen and proton cycles combine to help maintain a proton motive force?The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centreStructural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenaseHow the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenaseBacterial formate hydrogenlyase complexDistribution analysis of hydrogenases in surface waters of marine and freshwater environmentsPhysiology and bioenergetics of [NiFe]-hydrogenase 2-catalyzed H2-consuming and H2-producing reactions in Escherichia coli.Iron restriction induces preferential down-regulation of H(2)-consuming over H(2)-evolving reactions during fermentative growth of Escherichia coliHow oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases.Catalytic properties of the isolated diaphorase fragment of the NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha.A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.Zymographic differentiation of [NiFe]-hydrogenases 1, 2 and 3 of Escherichia coli K-12.Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarumAmino acid modified Ni catalyst exhibits reversible H2 oxidation/production over a broad pH range at elevated temperatures.Characterization of a unique [FeS] cluster in the electron transfer chain of the oxygen tolerant [NiFe] hydrogenase from Aquifex aeolicus.Metagenomic insights into S(0) precipitation in a terrestrial subsurface lithoautotrophic ecosystemHost hydrogen rather than that produced by the pathogen is important for Salmonella enterica serovar Typhimurium virulenceCrystallization and preliminary X-ray analysis of the NAD+-reducing [NiFe] hydrogenase from Hydrogenophilus thermoluteolus TH-1.Reversibility and efficiency in electrocatalytic energy conversion and lessons from enzymes.Metagenomic Sequencing Unravels Gene Fragments with Phylogenetic Signatures of O2-Tolerant NiFe Membrane-Bound Hydrogenases in Lacustrine SedimentActivation of formate hydrogen-lyase via expression of uptake [NiFe]-hydrogenase in Escherichia coli BL21(DE3)Electrocatalytic mechanism of reversible hydrogen cycling by enzymes and distinctions between the major classes of hydrogenases.Relation between anaerobic inactivation and oxygen tolerance in a large series of NiFe hydrogenase mutants.Genomic and metagenomic surveys of hydrogenase distribution indicate H2 is a widely utilised energy source for microbial growth and survivalH2 metabolism is widespread and diverse among human colonic microbesEnzymes as modular catalysts for redox half-reactions in H2-powered chemical synthesis: from biology to technology.Multiple and reversible hydrogenases for hydrogen production by Escherichia coli: dependence on fermentation substrate, pH and the F(0)F(1)-ATPase.Structure, function and biosynthesis of O₂-tolerant hydrogenases.Mechanisms for hydrogen production by different bacteria during mixed-acid and photo-fermentation and perspectives of hydrogen production biotechnology.Cyanobacterial hydrogenases and hydrogen metabolism revisited: recent progress and future prospectsHow the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure.Dual organism design cycle reveals small subunit substitutions that improve [NiFe] hydrogenase hydrogen evolution.Dissection and engineering of the Escherichia coli formate hydrogenlyase complex.Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C IntermediateRetuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.ArcA and AppY antagonize IscR repression of hydrogenase-1 expression under anaerobic conditions, revealing a novel mode of O2 regulation of gene expression in Escherichia coli.Role of the NiFe hydrogenase Hya in oxidative stress defense in Geobacter sulfurreducens.
P2860
Q26767154-8D28B0E8-2620-425B-8C2C-012D80A9B9ABQ26825963-498CD4BA-22B1-4EBD-B0DA-CE7DB83629DBQ27025185-97003FBF-4F3E-4C19-9094-2BE099162C75Q27675093-8CEE3163-B046-4BC1-B205-D1C98624FA79Q27675095-6CBD2EFD-A44A-4421-BCF6-C9CCF3A5D953Q27681350-ACB566E8-7CA9-4D3B-A78C-FBF6D22B73EFQ28655087-1F07A982-59B5-44F6-9288-64458161C035Q28748549-8876B077-A78C-4026-A398-E4EF7FFC33E8Q30316992-DE1B04D0-BA73-42CA-AA17-AEF02DAA2687Q30318317-6A5AE33F-4B8D-4626-8300-ED8E5AF5D427Q33607048-2DD7E91C-5E7F-461C-AD24-3A98D62006E3Q34053374-9AE87A8E-2697-43CD-8252-66209BE1972CQ34169576-8E8B7AF9-CC12-40B0-A5FE-C78A9766B893Q34329478-6C19E2D4-23AF-4F26-BC7F-FC8A23AE0180Q34470984-DF19016B-5B55-4BAC-92DA-E736AE465E08Q34581071-EAA942DC-5917-4E38-BE91-228F3012955DQ34794910-8402BA34-2596-49D4-9F76-861B1F350D14Q34881554-121D962B-09BD-4FE4-8D26-65694885D81BQ34889881-5E5334D5-7933-41F2-BCE4-D12C0957FA41Q35007022-B6B20B74-33E8-421B-9AEF-D09538A4CB5EQ35180570-E6850AC2-46BB-4371-BD11-D3855E2891ADQ35800502-BC047579-8572-41D5-8C54-9C7A8D4A438BQ36081765-8B40D1D3-7142-40A0-A2B1-F0630C53D265Q36122948-80776645-6017-41A2-92F0-10F7DF85A8D6Q36471139-29166D48-970C-4213-8137-DC08E46B535BQ36756517-14A97D8D-E8FF-4C81-80E1-621CFD11C7C7Q37082681-C3723247-7137-4285-8864-E8EE0E440A78Q37632855-AC133172-BD26-400E-8B85-B516E5AC2157Q37982137-73C6B269-A28E-4721-AB8B-C11AA49E217FQ38074265-7F48244B-2C38-4F5F-A338-BC0C70E9BCC1Q38124879-F0141C6A-37D9-4064-A973-7FA113A954EBQ38501371-F75AEBD9-1B0A-42FB-A00B-4398172FB1FDQ38685407-C11978E2-F8F9-4CA5-9AFB-57B4FA4E9BEEQ39392361-F9771885-372B-4FF5-B799-6743E7C73241Q40551697-BD8191EB-F61C-4B16-96CB-12D9D9332EA8Q41206125-0BC5D5CC-003D-4980-9C1E-E6D94D1A9C71Q41428109-C1BBF28E-0151-4537-A455-62BC3620295BQ41456603-9D96DC06-A65C-42A2-8D58-06FF2646BA47Q41783641-7E816B85-4182-4251-9B8B-D7BF1DB32823Q41847875-F0EC09AE-A683-498D-8AF3-DEE8BE5F49A9
P2860
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@en
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@nl
type
label
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@en
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@nl
prefLabel
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@en
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@nl
P2860
P50
P356
P1476
How Escherichia coli is equipped to oxidize hydrogen under different redox conditions.
@en
P2093
Fraser A Armstrong
Michael J Lukey
P2860
P304
P356
10.1074/JBC.M109.067751
P407
P577
2009-11-16T00:00:00Z