The cofactor of the iron-sulfur cluster free hydrogenase hmd: structure of the light-inactivation product.
about
Tricarbonylmanganese(I)-lysozyme complex: a structurally characterized organometallic proteinThe crystal structure of [Fe]-hydrogenase reveals the geometry of the active siteThe crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complexCrystal structures of [Fe]-hydrogenase in complex with inhibitory isocyanides: implications for the H2-activation siteIdentification of the HcgB enzyme in [Fe]-hydrogenase-cofactor biosynthesisProtein-pyridinol thioester precursor for biosynthesis of the organometallic acyl-iron ligand in [Fe]-hydrogenase cofactorTowards a functional identification of catalytically inactive [Fe]-hydrogenase paralogsIdentification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor BiosynthesisThe iron-sulfur cluster-free hydrogenase (Hmd) is a metalloenzyme with a novel iron binding motifCharacterization of the Fe site in iron-sulfur cluster-free hydrogenase (Hmd) and of a model compound via nuclear resonance vibrational spectroscopy (NRVS).Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor.Microbial CO conversions with applications in synthesis gas purification and bio-desulfurization.Evolution in the understanding of [Fe]-hydrogenase.[Fe]-hydrogenase and models that contain iron-acyl ligation.Radical S-adenosyl-L-methionine chemistry in the synthesis of hydrogenase and nitrogenase metal cofactors.Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH.The exchange activities of [Fe] hydrogenase (iron-sulfur-cluster-free hydrogenase) from methanogenic archaea in comparison with the exchange activities of [FeFe] and [NiFe] hydrogenases.Nature's hydrides: rapid reduction of halocarbons by folate model compoundsThe [Fe-Fe]-hydrogenase maturation protein HydF from Thermotoga maritima is a GTPase with an iron-sulfur cluster.The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of ralstonia eutropha H16 by way of a cyanide ligand to nickel.Fe4S4 Cubane Type Cluster Immobilized on a Graphene Support: A High Performance H2 Evolution Catalysis in Acidic Water.A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC.Reconstitution of [Fe]-hydrogenase using model complexes.Theoretical investigation of aerobic and anaerobic oxidative inactivation of the [NiFe]-hydrogenase active site.Reversible dimerization of mononuclear models of [Fe]-hydrogenase.Toward functional type III [Fe]-hydrogenase biomimics for H2 activation: insights from computation.Substitution reactions of iron(ii) carbamoyl-thioether complexes related to mono-iron hydrogenase.Towards artificial methanogenesis: biosynthesis of the [Fe]-hydrogenase cofactor and characterization of the semi-synthetic hydrogenase.Synthesis and reactivity of mononuclear iron models of [Fe]-hydrogenase that contain an acylmethylpyridinol ligand.
P2860
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P2860
The cofactor of the iron-sulfur cluster free hydrogenase hmd: structure of the light-inactivation product.
description
2004 nî lūn-bûn
@nan
2004 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
The cofactor of the iron-sulfu ...... he light-inactivation product.
@ast
The cofactor of the iron-sulfu ...... he light-inactivation product.
@en
The cofactor of the iron-sulfu ...... he light-inactivation product.
@nl
type
label
The cofactor of the iron-sulfu ...... he light-inactivation product.
@ast
The cofactor of the iron-sulfu ...... he light-inactivation product.
@en
The cofactor of the iron-sulfu ...... he light-inactivation product.
@nl
prefLabel
The cofactor of the iron-sulfu ...... he light-inactivation product.
@ast
The cofactor of the iron-sulfu ...... he light-inactivation product.
@en
The cofactor of the iron-sulfu ...... he light-inactivation product.
@nl
P2093
P356
P1476
The cofactor of the iron-sulfu ...... he light-inactivation product.
@en
P2093
Christian Griesinger
Erica J Lyon
Jörg Kahnt
Klaus Steinbach
Laurent Verdier
Manuela Kauss
Melanie Sordel-Klippert
Rudolf K Thauer
Seigo Shima
Xiulan Xie
P304
P356
10.1002/ANIE.200353763
P407
P577
2004-05-01T00:00:00Z