Carbamoylphosphate serves as the source of CN(-), but not of the intrinsic CO in the active site of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha.
about
Structure of [NiFe] Hydrogenase Maturation Protein HypE from Escherichia coli and Its Interaction with HypFX-ray structure of the [FeFe]-hydrogenase maturase HydE from Thermotoga maritimaStructural Basis for the Reaction Mechanism of S-Carbamoylation of HypE by HypF in the Maturation of [NiFe]-HydrogenasesStructural Basis for GTP-Dependent Dimerization of Hydrogenase Maturation Factor HypBThe influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation[NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins1.The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins.[NiFe]-hydrogenase maturation: isolation of a HypC-HypD complex carrying diatomic CO and CN- ligands.Metabolic deficiences revealed in the biotechnologically important model bacterium Escherichia coli BL21(DE3)Development of a cell-free system reveals an oxygen-labile step in the maturation of [NiFe]-hydrogenase 2 of Escherichia coli.Interaction between hydrogenase maturation factors HypA and HypB is required for [NiFe]-hydrogenase maturation.Dual role of HupF in the biosynthesis of [NiFe] hydrogenase in Rhizobium leguminosarumCrystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase.A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase.An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from Cupriavidus necator in Escherichia coliConcerted action of two novel auxiliary proteins in assembly of the active site in a membrane-bound [NiFe] hydrogenase.Cyanide and Carbon Monoxide Ligand Formation in Hydrogenase Biosynthesis
P2860
Q27649237-B97A554E-EEF1-4F03-9F30-1CDF0CB8CDD7Q27650297-10748204-9C58-496B-94CA-9E354AFE400CQ27670548-1178D20D-04B7-44FF-8714-DDFDDA29BE51Q27676885-3DA8199C-8C00-4E1B-B778-AC320D937095Q30317091-6C4CB49C-2A5D-43D9-A52D-948298F82B99Q30317101-5FEB4F63-F04D-495A-9816-2A2C25F8CEB0Q30317775-FAB9A726-B3AB-4CDE-BAC9-C63C0892F936Q30317985-BC979282-7448-42EC-8A09-F7BF8B244D41Q30318337-FB3E4758-3588-4A0F-ABCB-E4B50BBAB7D9Q30318589-992E58B5-E2D6-4C37-BB35-C97F0F759C41Q34182792-72D101EF-AD1F-4BE5-9AC8-EC7C1549DCEAQ34470984-9CDA81A8-C17A-4DF6-95AD-DB0C339041A1Q39969567-20740599-B5DC-4A49-B561-EDECF1E1FBE7Q40040482-5331DAF4-9269-4283-B67C-A5ADBE5E0546Q41310809-5B6EA748-F63A-4D48-9969-AD44AA538977Q42001721-31BB3C31-CA18-4030-B4D5-56903C33B2B4Q44491267-BF9857DC-498D-46E9-B0DC-D54D44BF29B0Q58879849-B9C7C9E4-0876-4517-BE1B-43EC43209843
P2860
Carbamoylphosphate serves as the source of CN(-), but not of the intrinsic CO in the active site of the regulatory [NiFe]-hydrogenase from Ralstonia eutropha.
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
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@en
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@nl
type
label
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@en
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@nl
prefLabel
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@en
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@nl
P2093
P2860
P1433
P1476
Carbamoylphosphate serves as t ...... enase from Ralstonia eutropha.
@en
P2093
Bärbel Friedrich
Ingo Zebger
Josta Hamann
P2860
P304
P356
10.1016/J.FEBSLET.2007.06.027
P407
P577
2007-06-21T00:00:00Z