The [4Fe‐4S]‐Cluster of HydF is not Required for the Binding and Transfer of the Diiron Site of [FeFe]‐Hydrogenases
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DOI: 10.1002/cbic.202300222
Abstract: The active site of [FeFe]‐hydrogenases contains a cubane [4Fe‐4S]‐cluster and a unique diiron cluster with biologically unusual CO and CN− ligands. The biogenesis of this diiron site, termed [2FeH], requires the maturation proteins HydE, HydF… read more here.
Keywords: transfer; hydf; site; cluster ... See more keywords
Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch
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DOI: 10.1038/s41598-017-01886-y
Abstract: Abstract[FeFe]-hydrogenases catalyse the reduction of protons to hydrogen at a complex 2Fe[4Fe4S] center called H-cluster. The assembly of this active site is a multistep process involving three proteins, HydE, HydF and HydG. According to the… read more here.
Keywords: site directed; gtpase domain; cluster; domain ... See more keywords