Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.
about
Structure-function relationships in [FeFe]-hydrogenase active site maturationStepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG)Crystal Structure of HydF Scaffold Protein Provides Insights into [FeFe]-Hydrogenase MaturationTyrosine, cysteine, and S-adenosyl methionine stimulate in vitro [FeFe] hydrogenase activationIron-sulfur cluster coordination in the [FeFe]-hydrogenase H cluster biosynthetic factor HydFFeoC from Klebsiella pneumoniae contains a [4Fe-4S] cluster[NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins1.Development of a cell-free system reveals an oxygen-labile step in the maturation of [NiFe]-hydrogenase 2 of Escherichia coli.In silico evaluation of proposed biosynthetic pathways for the unique dithiolate ligand of the H-cluster of [FeFe]-hydrogenase.High-yield expression of heterologous [FeFe] hydrogenases in Escherichia coli.Emerging themes in radical SAM chemistryA Redox Active [2Fe-2S] Cluster on the Hydrogenase Maturase HydF.Synthesis of the 2Fe subcluster of the [FeFe]-hydrogenase H cluster on the HydF scaffold.Cysteine as a ligand platform in the biosynthesis of the FeFe hydrogenase H cluster.EPR Spectroscopic Studies of [FeFe]-Hydrogenase Maturation.Structural diversity in the AdoMet radical enzyme superfamily.Biosynthesis of the [FeFe] Hydrogenase H Cluster: A Central Role for the Radical SAM Enzyme HydGSpectroscopic Investigations of [FeFe] Hydrogenase Maturated with [(57)Fe2(adt)(CN)2(CO)4](2-)PqqE from Methylobacterium extorquens AM1: a radical S-adenosyl-l-methionine enzyme with an unusual tolerance to oxygen.Radical S-adenosylmethionine enzymes.Structural insights into radical generation by the radical SAM superfamily.H-cluster assembly during maturation of the [FeFe]-hydrogenase.Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.Importance of the protein framework for catalytic activity of [FeFe]-hydrogenases.A New Route to Azadithiolato ComplexesBiochemical analysis of the interactions between the proteins involved in the [FeFe]-hydrogenase maturation process.[FeFe]-hydrogenase cyanide ligands derived from S-adenosylmethionine-dependent cleavage of tyrosine.The [FeFe]-hydrogenase maturase HydF from Clostridium acetobutylicum contains a CO and CN- ligated iron cofactor.Electron Spin Relaxation and Biochemical Characterization of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S] Cluster Communication and Hydrogenase Activation.Characterization of auxiliary iron-sulfur clusters in a radical S-adenosylmethionine enzyme PqqE from Methylobacterium extorquens AM1.Compartmentalisation of [FeFe]-hydrogenase maturation in Chlamydomonas reinhardtii.[FeFe]-Hydrogenase with Chalcogenide Substitutions at the H-Cluster Maintains Full H2 Evolution Activity.A structural view of synthetic cofactor integration into [FeFe]-hydrogenases.Influence of the [4Fe-4S] cluster coordinating cysteines on active site maturation and catalytic properties of C. reinhardtii [FeFe]-hydrogenase.
P2860
Q26864249-A2C5EB10-CEBA-4235-A884-6B1119AFE6F8Q27660863-B424149B-1CBB-49D4-9D6B-A9B48760BA08Q27675419-21B7A4D0-9B0C-4C4E-8B9B-EC743C4B2AAFQ28471581-447001ED-74AF-4063-B270-EFA2BA458D18Q28485894-B1CEFE7E-1ACC-4C5F-8282-EE210ADBD1D8Q28662158-8A94077A-A9AA-4D98-AD1D-C4F975631C0BQ30317101-82F1BB64-8056-4EDC-BB4B-AE58252B40ABQ30318589-46EB570E-733A-4F94-A7A7-A127664F1720Q33352221-FF17BE31-F560-483F-B286-B4F97CBA7049Q33760762-F605A899-536E-42A9-83F1-4691554993D5Q33851840-B464F9B1-9D2C-44F0-BCD2-46DB7D84D9D1Q33885103-113D2F68-C534-4DA0-B30B-6BA4DC25DF9EQ33935037-E2F0A9C9-0E4D-4114-887C-FEDE77BABED2Q36079128-7E52FDF1-78A8-458D-AE14-08800C725923Q36200898-88E74B10-84BC-4DEF-8D37-A38DF90BD4B3Q36469251-135417E8-0E2D-46D8-BEFB-CD80207268ABQ36659198-5BBDC315-BFA2-4B49-B4DE-69DEB3ED90DAQ36706563-43B89A01-30E7-4326-A765-DC06E19F1D70Q36941648-337F7C92-3E11-4DCA-B6CD-556BC92AA51CQ37727698-A09865CF-2886-454F-901B-95EA72064715Q37849296-5727855E-3D6A-49DD-BAB8-16EB86F9E8EDQ38223922-BF4A9D4E-C209-4562-B493-5965CA7BB3D5Q38283509-4D4C6FDE-8A14-41D1-ACA8-135E004416C3Q40355157-7C2C4ED5-C24A-4602-A6F6-16C5FAE235AFQ41533113-C53BCEE1-3749-46C8-8C1B-DAE6089DF807Q42120050-BFC40623-55A0-4875-AD15-FA74EB2B1DC2Q43182197-0169141F-6D9F-469B-9929-CB7429718A9AQ45189933-CB662BDA-BA85-4328-85CD-7BBFFCE3439CQ46363546-75C23A16-C8A9-400C-9E3C-8347B37F1792Q47107286-A6F4AD66-3C03-4DD1-9235-31F5045790F6Q50205913-5D3653A3-5564-4FFE-A568-B851D177265CQ53083787-2B82CF29-9FCE-45A4-BA56-E8CE0B7E110AQ55275293-44295AA4-8AA2-43D3-BC4F-1F1DA514EFD8Q55347805-7C376879-9589-4B14-97BD-2AF685CC2C04
P2860
Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.
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
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-hant
name
Activation of HydA
@nl
Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.
@en
type
label
Activation of HydA
@nl
Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.
@en
prefLabel
Activation of HydA
@nl
Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.
@en
P2093
P356
P1433
P1476
Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster.
@en
P2093
Anatoli V Naumov
BoiHanh Huynh
Danilo O Ortillo
David J Gardenghi
David W Mulder
John W Peters
Shane S Ruebush
P304
P356
10.1021/BI9000563
P407
P577
2009-07-01T00:00:00Z