A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase. - Wikidata - awgldk - TriplyDB

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

http://www.wikidata.org/entity/Q34169576

about

Electrochemical insights into the mechanism of NiFe membrane-bound hydrogenases NAD(H)-coupled hydrogen cycling - structure-function relationships of bidirectional [NiFe] hydrogenases The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centre Structural basis for a [4Fe-3S] cluster in the oxygen-tolerant membrane-bound [NiFe]-hydrogenase X-ray crystallographic and computational studies of the O2-tolerant [NiFe]-hydrogenase 1 from Escherichia coli How the structure of the large subunit controls function in an oxygen-tolerant [NiFe]-hydrogenase Reversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenase [NiFe]-hydrogenases revisited: nickel-carboxamido bond formation in a variant with accrued O2-tolerance and a tentative re-interpretation of Ni-SI states hypD as a marker for [NiFe]-hydrogenases in microbial communities of surface waters Design and development of synthetic microbial platform cells for bioenergy How oxygen reacts with oxygen-tolerant respiratory [NiFe]-hydrogenases.A Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF.Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarum An analysis of the changes in soluble hydrogenase and global gene expression in Cupriavidus necator (Ralstonia eutropha) H16 grown in heterotrophic diauxic batch culture.Cultivation-independent detection of autotrophic hydrogen-oxidizing bacteria by DNA stable-isotope probing.Regioselectivity of H cluster oxidation.Metagenomic Sequencing Unravels Gene Fragments with Phylogenetic Signatures of O2-Tolerant NiFe Membrane-Bound Hydrogenases in Lacustrine Sediment Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase.Mechanistic insight into the blocking of CO diffusion in [NiFe]-hydrogenase mutants through multiscale simulation.Lyophilization protects [FeFe]-hydrogenases against O2-induced H-cluster degradation.New iron-sulfur clusters help hydrogenases tolerate oxygen.Electronic structure of the unique [4Fe-3S] cluster in O2-tolerant hydrogenases characterized by 57Fe Mossbauer and EPR spectroscopy.Distribution of Hydrogenases in Cyanobacteria: A Phylum-Wide Genomic Survey.Developments in the biomimetic chemistry of cubane-type and higher nuclearity iron-sulfur clusters.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers Studies on hydrogenase.Structure, function and biosynthesis of O₂-tolerant hydrogenases.Rubredoxin-related maturation factor guarantees metal cofactor integrity during aerobic biosynthesis of membrane-bound [NiFe] hydrogenase How the oxygen tolerance of a [NiFe]-hydrogenase depends on quaternary structure.Structure and function of [NiFe] hydrogenases.O2 reactions at the six-iron active site (H-cluster) in [FeFe]-hydrogenase Dual organism design cycle reveals small subunit substitutions that improve [NiFe] hydrogenase hydrogen evolution.Dissection and engineering of the Escherichia coli formate hydrogenlyase complex.A broad survey reveals substitution tolerance of residues ligating FeS clusters in [NiFe] hydrogenase.Re-engineering a NiFe hydrogenase to increase the H2 production bias while maintaining native levels of O2 tolerance.Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha.Discovery of Dark pH-Dependent H(+) Migration in a [NiFe]-Hydrogenase and Its Mechanistic Relevance: Mobilizing the Hydrido Ligand of the Ni-C Intermediate Retuning the Catalytic Bias and Overpotential of a [NiFe]-Hydrogenase via a Single Amino Acid Exchange at the Electron Entry/Exit Site.Photocatalytic hydrogen evolution with a hydrogenase in a mediator-free system under high levels of oxygen Infrared Spectroscopy During Electrocatalytic Turnover Reveals the Ni-L Active Site State During H2 Oxidation by a NiFe Hydrogenase.

P2860

Q26767154-9D83EA1D-F413-4FC0-9780-9A8441D84E7F Q27011364-47F40F6D-C7C5-4C34-AF5B-F66A512AC10B Q27675093-A20B0474-0156-4212-85ED-687D920357E2 Q27675095-BAFFB38A-0507-495B-B231-3DA56DA70B9A Q27678099-DE971A98-3DA4-4C20-9E0E-0207AB525F48 Q27681350-E4BFE9B4-2D4D-4C19-BACC-7D6BA312551C Q27690017-412E283E-FF06-46F6-BF13-B56108BE4D0A Q27698514-5327FD23-41D6-4C5E-A615-C6770845ADA2 Q28658334-9C62EF66-5C54-43FD-B8AB-A4904C7031DB Q28708939-F14096AD-8A47-4F08-B3A9-4F37B407912B Q33607048-0D0B1E13-315E-4116-AA5E-A75FDC7179B9 Q33885103-08A749B8-E87D-474C-BB24-357CA209C770 Q34470984-6B994422-0E00-495A-BB3D-526137C05C90 Q34472066-9FB0C492-83EE-4E38-BC57-F8D14FFFF7D4 Q35138861-B80A6D3B-54A2-4EF9-B5FA-61301D98D1D3 Q35615181-9154F72B-1995-42BF-8176-573FE3C49AA5 Q35800502-709587DC-B5BD-4370-A6DB-832F41241FF0 Q35845365-161B0AAC-9591-4317-9B38-E2861172C144 Q35921991-DF9DBC2F-9492-4949-A860-D5CD12547BC5 Q36056328-994D07D4-2599-4EB7-8FEC-28A6AD55619C Q36301059-0D5AE253-6DB9-47B0-A881-1622335CE8A4 Q36535414-25B929D2-8B9B-49A3-AACB-EFF6C9AE89EF Q37532901-0FFD156B-85D2-403B-BBF4-94B8EBCD917D Q37696184-D3140600-14CC-4698-AC42-CCDB8CC96784 Q37727718-6FF184FE-28BA-480E-9A1A-2344DE1289AF Q38074042-5E626B55-F195-47C1-9036-14D6199958D0 Q38074265-C7563FF0-9431-4CEE-98AD-03D685EBD824 Q38268409-E3F54620-58BD-4345-8A89-86DFFEBF321D Q38685407-A18C0129-4858-4EE6-A6FB-46F6AB13AE98 Q38919272-3FC535C5-C63B-448B-A5F0-8CDFA6AF6062 Q39242075-DB2A6007-DFF7-40E0-80D9-EE929FB9AFF8 Q39392361-72348CB3-0256-4BF5-82A1-C8402272CBC7 Q40551697-0E274B17-2E90-4A8B-9588-0D098C45CEB9 Q41144081-C86A9906-1C96-4B9F-8DDB-DC58BB607BAB Q41206125-7D66A15D-A97B-40A4-8804-C23BF08EA867 Q41387381-E5429AB8-513E-482F-93F1-939C44C810CF Q41428109-D6F11E61-5941-4DF5-8195-483B945CF186 Q41456603-A56D4C46-9AC2-4199-8B48-AFC7C18BEB82 Q41866485-F6BAF6EC-DC14-4A34-951E-04A1566FC9CA Q41888921-A6DBB2BB-B64A-4087-BEC0-AF3715A27376

P2860

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

http://www.wikidata.org/entity/Q34169576

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@ast

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@en

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@nl

type

label

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@ast

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@en

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@nl

prefLabel

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@ast

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@en

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@nl

P1433

Q34169576-03F45E6F-15D6-46FB-9D0B-B26FF99EBA7D

P1476

Q34169576-1E5DF889-AD06-4606-A414-4CB7891C9818

P2093

Q34169576-0F4E269C-EEF5-41BF-A1A4-BB2F693898D7

Q34169576-2472DA44-D335-41C2-86FE-07F85DBB80D8

Q34169576-3807AF6C-88B5-4180-B5E9-EBE97751B3C7

Q34169576-3DE04776-8729-4220-85C9-DA862189AE32

Q34169576-40CB25A0-C2BE-465E-B31A-5B8774A5149F

Q34169576-B8F84E31-5549-4E71-89CD-927D790AF0D1

Q34169576-D498E310-9A06-477F-AC87-494A6A52B1EF

P2860

Q34169576-03D0C62A-47CD-4B42-871A-A5BC7FD0AFCF

Q34169576-05D800A4-7DFC-49D1-B3AB-3139CD49B4AC

Q34169576-0706AD50-3C6A-4E3F-B0BE-7DFCD2E6EC02

Q34169576-09676A4B-ADF8-453E-8301-BC321FCD9E5D

Q34169576-1957769A-4A53-45A7-AEAA-936B066CED12

Q34169576-264A7D6C-C3DD-4E2F-AE33-E82CDF9A86D2

Q34169576-2E0CB8B0-8E81-46FE-B6BA-1844A151D144

Q34169576-38455437-19DA-4EFD-885D-A47DF4AA584D

Q34169576-4838C484-C328-4501-B4D9-BD25AFB33296

Q34169576-4B429911-F2C7-4326-878E-E70A0E8FB72E

P2888

Q34169576-A73BB06E-2AF8-4EB1-8D50-207AE494850A

P304

Q34169576-DBC075E4-32FC-4AF0-A5A3-0E5EA881DD6D

P31

Q34169576-438C5EFB-EE59-4DD0-B660-AD1DF26C8614

P356

Q34169576-4A6990DB-5DE2-40D5-B759-9BE23D43E698

P433

Q34169576-CD7A5C0C-7B84-4B65-A6A7-5B8F90D5EC30

P478

Q34169576-9902F72F-1DDC-4F3F-A598-79373E7F197E

P50

Q34169576-404B1C88-772A-43A5-A156-7C38193FD92A

Q34169576-73F06BD4-A462-4618-B235-9460760BFCBA

Q34169576-9F56F9F7-12DA-4657-8A33-CBD3174A133C

Q34169576-BD229140-A4AD-417C-8448-59102E3B6EB1

P577

Q34169576-95188C2B-92F1-455B-A0E2-A316BD2D72C7

P5875

Q34169576-BD478B5F-9CDF-44EE-9E65-DA3ED6A4E71B

P6179

Q34169576-F3483D40-11C3-4DBD-B36A-945CB558B0B6

P698

Q34169576-D7BD1EB4-0A5C-4F34-B4B7-C3FEA0E2EDDA

P356

P1433

Nature Chemical Biology

P1476

A unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.

@en

P2093

Annemarie F Wait

http://www.w3.org/2001/XMLSchema#string

Bärbel Friedrich

http://www.w3.org/2001/XMLSchema#string

Fraser A Armstrong

http://www.w3.org/2001/XMLSchema#string

Johannes Fritsch

http://www.w3.org/2001/XMLSchema#string

Matthias Stein

http://www.w3.org/2001/XMLSchema#string

Nina Heidary

http://www.w3.org/2001/XMLSchema#string

Oliver Lenz

http://www.w3.org/2001/XMLSchema#string

P2860

Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levels

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Experimental approaches to kinetics of gas diffusion in hydrogenase

Structural Basis for the Mechanism of Respiratory Complex I

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

Comparative protein modelling by satisfaction of spatial restraints

[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation

Functional and structural role of the cytochrome b subunit of the membrane-bound hydrogenase complex of Alcaligenes eutrophus H16

Structure-function relationships of anaerobic gas-processing metalloenzymes

The Universal Protein Resource (UniProt) in 2010

P2888

P304

310-318

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1038/NCHEMBIO.555

http://www.w3.org/2001/XMLSchema#string

P433

5

http://www.w3.org/2001/XMLSchema#string

P478

7

http://www.w3.org/2001/XMLSchema#string

P50

Friedhelm Lendzian

P577

2011-03-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

50352035

http://www.w3.org/2001/XMLSchema#string

P6179

1038338434

http://www.w3.org/2001/XMLSchema#string

P698

21390036

http://www.w3.org/2001/XMLSchema#string