Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum
about
From volcanic origins of chemoautotrophic life to Bacteria, Archaea and EukaryaThe crystal structure of [Fe]-hydrogenase reveals the geometry of the active siteIron-sulfur cluster coordination in the [FeFe]-hydrogenase H cluster biosynthetic factor HydFBiohydrogen Production by the Thermophilic Bacterium Caldicellulosiruptor saccharolyticus: Current Status and PerspectivesStepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamicsMolecular dynamics and experimental investigation of H(2) and O(2) diffusion in [Fe]-hydrogenase.Cysteine residue 911 in C-terminal tail of human BK(Ca)α channel subunit is crucial for its activation by carbon monoxide.Carbon monoxide: an emerging regulator of ion channels.Learning from hydrogenases: location of a proton pump and of a second FMN in bovine NADH--ubiquinone oxidoreductase (Complex I).2,4,6-trinitrotoluene reduction by an Fe-only hydrogenase in Clostridium acetobutylicumThe organometallic active site of [Fe]hydrogenase: models and entatic states.How oxygen attacks [FeFe] hydrogenases from photosynthetic organisms.[Fe-Fe]-hydrogenase Reactivated by Residue Mutations as Bridging Carbonyl Rearranges: A QM/MM Study.Spectroscopic Investigations of [FeFe] Hydrogenase Maturated with [(57)Fe2(adt)(CN)2(CO)4](2-)Radical S-adenosylmethionine enzymes.De novo design of functional proteins: Toward artificial hydrogenases.Bioinspired Hydrogenase Models: The Mixed-Valence Triiron Complex [Fe3(CO)7(μ-edt)2] and Phosphine Derivatives [Fe3(CO)7-x (PPh3) x (μ-edt)2] (x = 1, 2) and [Fe3(CO)5(κ(2)-diphosphine)(μ-edt)2] as Proton Reduction Catalysts.Hydrogenase Enzymes and Their Synthetic Models: The Role of Metal Hydrides.Towards [NiFe]-hydrogenase biomimetic models that couple H2 binding with functionally relevant intramolecular electron transfers: a quantum chemical study.Diiron dithiolato carbonyls related to the H(ox)CO state of [FeFe]-hydrogenase.Artificially maturated [FeFe] hydrogenase from Chlamydomonas reinhardtii: a HYSCORE and ENDOR study of a non-natural H-cluster.NADP-specific electron-bifurcating [FeFe]-hydrogenase in a functional complex with formate dehydrogenase in Clostridium autoethanogenum grown on CO.Carbon monoxide as an electron donor for the biological reduction of sulphateDoes the environment around the H-cluster allow coordination of the pendant amine to the catalytic iron center in [FeFe] hydrogenases? Answers from theory.Biomimetic model for [FeFe]-hydrogenase: asymmetrically disubstituted diiron complex with a redox-active 2,2'-bipyridyl ligand.Diiron species containing a cyclic P(Ph)2N(Ph)2 diphosphine related to the [FeFe]H2ases active site.Protonation/reduction dynamics at the [4Fe-4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases.Chalcogenide substitution in the [2Fe] cluster of [FeFe]-hydrogenases conserves high enzymatic activity.Bridgehead isomer effects in bis(phosphido)-bridged diiron hexacarbonyl proton reduction electrocatalysts.Photoswitchable electrochemical behaviour of a [FeFe] hydrogenase model with a dithienylethene derivative.Hyperfine interactions and electron distribution in Fe(II)Fe (I) and Fe (I)Fe (I) models for the active site of the [FeFe] hydrogenases: Mössbauer spectroscopy studies of low-spin Fe(I.).[FeFe]-Hydrogenase H-Cluster Mimics with Unique Planar μ-(SCH2 )2 ER2 Linkers (E=Ge and Sn).Bio-inspired hydrogenase models: mixed-valence triion complexes as proton reduction catalysts.Synthesis, characterization, and electrochemical properties of diiron propaneditellurolate (PDTe) complexes as active site models of [FeFe]-hydrogenases.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.Hydrogenases and oxygen
P2860
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P2860
Binding of exogenously added carbon monoxide at the active site of the iron-only hydrogenase (CpI) from Clostridium pasteurianum
description
1999 nî lūn-bûn
@nan
1999 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Binding of exogenously added c ...... from Clostridium pasteurianum
@ast
Binding of exogenously added c ...... from Clostridium pasteurianum
@en
Binding of exogenously added c ...... from Clostridium pasteurianum
@nl
type
label
Binding of exogenously added c ...... from Clostridium pasteurianum
@ast
Binding of exogenously added c ...... from Clostridium pasteurianum
@en
Binding of exogenously added c ...... from Clostridium pasteurianum
@nl
prefLabel
Binding of exogenously added c ...... from Clostridium pasteurianum
@ast
Binding of exogenously added c ...... from Clostridium pasteurianum
@en
Binding of exogenously added c ...... from Clostridium pasteurianum
@nl
P356
P1433
P1476
Binding of exogenously added c ...... from Clostridium pasteurianum
@en
P2093
P304
P356
10.1021/BI9913193
P407
P577
1999-10-05T00:00:00Z