Evidence from Mössbauer Spectroscopy for Distinct [2Fe-2S](2+) and [4Fe-4S](2+) Cluster Binding Sites in Biotin Synthase from Escherichia coli

Eitemau Tebyg

• Iron-Sulfur Cluster Interconversions in Biotin Synthase: Dissociation and Reassociation of Iron during Conversion of [2Fe-2S] to [4Fe-4S] Clusters()
  gan: Ugulava, Natalia B., et al.
  Cyhoeddwyd: (2000)
• Spectroscopic Changes during a Single Turnover of Biotin Synthase: Destruction of a [2Fe-2S] Cluster Accompanies Sulfur Insertion()
  gan: Ugulava, Natalia B., et al.
  Cyhoeddwyd: (2001)
• Biotin Synthase Contains Two Distinct Iron-Sulfur Cluster Binding Sites: Chemical and Spectroelectrochemical Analysis of Iron-Sulfur Cluster Interconversions()
  gan: Ugulava, Natalia B., et al.
  Cyhoeddwyd: (2001)
• The Role of the [2Fe-2S](2+) Cluster in Biotin Synthase: Mutagenesis of the Atypical Metal Ligand Arginine 260
  gan: Broach, Robyn B., et al.
  Cyhoeddwyd: (2006)
• Reduction of the [2Fe-2S] Cluster Accompanies Formation of the Intermediate 9-Mercaptodethiobiotin in Escherichia coli Biotin Synthase()
  gan: Taylor, Andrew M., et al.
  Cyhoeddwyd: (2011)