about
The crystal structure of an oxygen-tolerant hydrogenase uncovers a novel iron-sulphur centreReversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenaseKrypton Derivatization of an O2 -Tolerant Membrane-Bound [NiFe] Hydrogenase Reveals a Hydrophobic Tunnel Network for Gas TransportA stromal pool of TatA promotes Tat-dependent protein transport across the thylakoid membrane.Unassisted membrane insertion as the initial step in DeltapH/Tat-dependent protein transport.Double-flow focused liquid injector for efficient serial femtosecond crystallography.CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase.Enhanced oxygen-tolerance of the full heterotrimeric membrane-bound [NiFe]-hydrogenase of Ralstonia eutropha.Essential amino acid residues of BioY reveal that dimers are the functional S unit of the Rhodobacter capsulatus biotin transporter.Resonance Raman spectroscopy as a tool to monitor the active site of hydrogenases.Reactivation from the Ni-B state in [NiFe] hydrogenase of Ralstonia eutropha is controlled by reduction of the superoxidised proximal cluster.Tracking the route of molecular oxygen in O2-tolerant membrane-bound [NiFe] hydrogenase.A trimeric supercomplex of the oxygen-tolerant membrane-bound [NiFe]-hydrogenase from Ralstonia eutropha H16.Resonance Raman Spectroscopic Analysis of the [NiFe] Active Site and the Proximal [4Fe-3S] Cluster of an O2-Tolerant Membrane-Bound Hydrogenase in the Crystalline StateIn Situ Spectroelectrochemical Studies into the Formation and Stability of Robust Diazonium-Derived Interfaces on Gold Electrodes for the Immobilization of an Oxygen-Tolerant HydrogenaseRole of the HoxZ Subunit in the Electron Transfer Pathway of the Membrane-Bound [NiFe]-Hydrogenase fromRalstonia eutrophaImmobilized on ElectrodesO2-tolerant [NiFe]-hydrogenases of Ralstonia eutropha H16: Physiology, molecular biology, purification, and biochemical analysisA membrane-bound [NiFe]-hydrogenase large subunit precursor whose C-terminal extension is not essential for cofactor incorporation but guarantees optimal maturationO2-Tolerant H2 Activation by an Isolated Large Subunit of a [NiFe] HydrogenaseFormyltetrahydrofolate Decarbonylase Synthesizes the Active Site CO Ligand of O2-Tolerant [NiFe] Hydrogenase
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description
hulumtues
@sq
onderzoeker
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researcher
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ricercatore
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taighdeoir
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հետազոտող
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name
Stefan Frielingsdorf
@ast
Stefan Frielingsdorf
@en
Stefan Frielingsdorf
@es
Stefan Frielingsdorf
@nl
Stefan Frielingsdorf
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type
label
Stefan Frielingsdorf
@ast
Stefan Frielingsdorf
@en
Stefan Frielingsdorf
@es
Stefan Frielingsdorf
@nl
Stefan Frielingsdorf
@sl
prefLabel
Stefan Frielingsdorf
@ast
Stefan Frielingsdorf
@en
Stefan Frielingsdorf
@es
Stefan Frielingsdorf
@nl
Stefan Frielingsdorf
@sl
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0000 0000 5896 2318
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P31
P496
0000-0002-4141-7836
P569
1979-01-01T00:00:00Z
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P7859
viaf-86037811