Cell-free H-cluster Synthesis and [FeFe] Hydrogenase Activation: All Five CO and CN− Ligands Derive from Tyrosine
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Title
Cell-free H-cluster Synthesis and [FeFe] Hydrogenase Activation: All Five CO and CN− Ligands Derive from Tyrosine
Authors
Keywords
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Journal
PLoS One
Volume 6, Issue 5, Pages e20346
Publisher
Public Library of Science (PLoS)
Online
2011-06-01
DOI
10.1371/journal.pone.0020346
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Note: Only part of the references are listed.- [FeFe]-Hydrogenase Cyanide Ligands Derived From S-Adenosylmethionine-Dependent Cleavage of Tyrosine
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- The [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe4S]-2Fe site
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- Structural and Functional Analogues of the Active Sites of the [Fe]-, [NiFe]-, and [FeFe]-Hydrogenases†
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- The [FeFe]-hydrogenase maturase HydF fromClostridium acetobutylicumcontains a CO and CN−ligated iron cofactor
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- From Hydrogenases to Noble Metal-Free Catalytic Nanomaterials for H2 Production and Uptake
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- Deletion of iscR stimulates recombinant clostridial Fe–Fe hydrogenase activity and H2-accumulation in Escherichia coli BL21(DE3)
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- Dithiomethylether as a Ligand in the Hydrogenase H-Cluster
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