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  1. Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli
  2. Binding of a [2Fe–2S] cluster drives dimerization of ferric uptake regulator (Fur) in Escherichia coli
  3. Iron–sulfur cluster assembly scaffold protein IscU is required for activation of ferric uptake regulator (Fur) in Escherichia coli
  4. Ferric uptake regulator (Fur) binds a [2Fe-2S] cluster to regulate intracellular iron homeostasis in Escherichia coli
  5. Electron transfer activity of the nanodisc-bound mitochondrial outer membrane protein mitoNEET
  6. Ferric uptake regulators (Fur) from Vibrio cholerae and Helicobacter pylori bind a [2Fe–2S] cluster in response to elevation of intracellular free iron content
  7. Ferric uptake regulator (Fur) reversibly binds a [2Fe-2S] cluster to sense intracellular iron homeostasis in Escherichia coli
  8. Light-induced release of nitric oxide from the nitric oxide-bound CDGSH-type [2Fe–2S] clusters in mitochondrial protein Miner2
  9. Zinc Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli
  10. Electron transfer kinetics of the mitochondrial outer membrane protein mitoNEET
  11. Anaerobic Copper Toxicity and Iron-Sulfur Cluster Biogenesis in Escherichia coli
  12. The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH 2 to oxygen or ubiquinone
  13. Binding of nitric oxide in the CDGSH-type [2Fe-2S] clusters of human mitochondrial protein Miner2
  14. Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET
  15. Deletion of the Proposed Iron Chaperones IscA/SufA Results in Accumulation of a Red Intermediate Cysteine Desulfurase IscS in Escherichia coli
  16. Reduction of mitochondrial protein mitoNEET [2Fe–2S] clusters by human glutathione reductase
  17. Helicase and Its Interacting Factors: Regulation Mechanism, Characterization, Structure, and Application for Drug Design
  18. Dynamic Metabolism of Iron-Sulfur Proteins in Response to Nitric Oxide in Rat Heart Muscle Cells
  19. Redox Control of Mitochondrial Outer Membrane Protein MitoNEET Iron-Sulfur Clusters
  20. Copper binding in IscA inhibits iron-sulphur cluster assembly inEscherichia coli
  21. Iron and zinc binding activity of Escherichia coli topoisomerase I homolog YrdD
  22. Redox Control of Human Mitochondrial Outer Membrane Protein MitoNEET [2Fe-2S] Clusters by Biological Thiols and Hydrogen Peroxide
  23. The N-Terminal Domain of Human DNA Helicase Rtel1 Contains a Redox Active Iron-Sulfur Cluster
  24. Regulation of the Mitochondrial Protein mitoNEET [2Fe-2S] Cluster by Nitric Oxide
  25. Iron binding activity is essential for the function of IscA in iron–sulphur cluster biogenesis
  26. Stimulation ofEscherichia coliDNA damage inducible DNA helicase DinG by the single-stranded DNA binding protein SSB
  27. Competition of zinc ion for the [2Fe–2S] cluster binding site in the diabetes drug target protein mitoNEET
  28. Iron–sulfur proteins are the major source of protein-bound dinitrosyl iron complexes formed in Escherichia coli cells under nitric oxide stress
  29. Escherichia coli topoisomerase I is an iron and zinc binding protein
  30. In vivo evidence for the iron-binding activity of an iron–sulfur cluster assembly protein IscA in Escherichia coli
  31. Oxygen is required for the l-cysteine-mediated decomposition of protein-bound dinitrosyl–iron complexes
  32. Iron-binding activity of human iron–sulfur cluster assembly protein hIscA1
  33. Cellular Repair Mechanism for Protein-Bound Dinitrosyl Iron Complexes
  34. Ironsulfur Proteins Comprise the Major Source of Protein-bound Dinitrosyl Iron Complexes Formed in Escherichia coli Cells under Nitric Oxide Stress
  35. IscA/SufA paralogues are required for the [4Fe-4S] cluster assembly in enzymes of multiple physiological pathways in Escherichia coli under aerobic growth conditions
  36. Reactivity of nitric oxide with the [4Fe–4S] cluster of dihydroxyacid dehydratase from Escherichia coli
  37. Redox Control of the DNA Damage-inducible Protein DinG Helicase Activity via Its Iron-Sulfur Cluster
  38. Nitric oxide-induced bacteriostasis and modification of iron-sulphur proteins inEscherichia coli
  39. Escherichia coli FtnA acts as an iron buffer for re-assembly of iron–sulfur clusters in response to hydrogen peroxide stress
  40. Complementary roles of SufA and IscA in the biogenesis of iron–sulfur clusters in Escherichia coli
  41. Distinct Iron Binding Property of Two Putative Iron Donors for the Iron-Sulfur Cluster Assembly: IscA AND THE BACTERIAL FRATAXIN ORTHOLOG CyaY UNDER PHYSIOLOGICAL AND OXIDATIVE STRESS CONDITIONS
  42. Harnessing toxic reactions to signal stress: reactions of nitric oxide with iron–sulfur centers and the informative case of SoxR protein
  43. Interplay of IscA and IscU in Biogenesis of Iron-Sulfur Clusters
  44. Mobilization of the iron centre in IscA for the iron–sulphur cluster assembly in IscU
  45. Thioredoxin Reductase System Mediates Iron Binding in IscA and Iron Delivery for the Iron-Sulfur Cluster Assembly in IscU
  46. IscA Mediates Iron Delivery for Assembly of Iron-Sulfur Clusters in IscU under the Limited Accessible Free Iron Conditions
  47. Characterization of iron binding in IscA, an ancient iron-sulphur cluster assembly protein
  48. Crystal Structure of the Ancient, Fe−S Scaffold IscA Reveals a Novel Protein Fold †
  49. Reversible inactivation of E. coli endonuclease III via modification of its [4Fe-4S] cluster by nitric oxide
  50. Repair of Nitric Oxide-modified Ferredoxin [2Fe-2S] Cluster by Cysteine Desulfurase (IscS)
  51. [35] Escherichia coli SoxR protein: Sensor/transducer of oxidative stress and nitric oxide
  52. [4] Analyzing cotranslational protein folding and disulfide formation by diagonal sodium dodecyl sulfate-polyacrylamide gel electrophoresis
  53. L-Cysteine-mediated Destabilization of Dinitrosyl Iron Complexes in Proteins
  54. Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator
  55. 9. Transcriptional regulation via redox-sensitive iron-sulphur centres in an oxidative stress response
  56. Thiol-Mediated Disassembly and Reassembly of [2Fe-2S] Clusters in the Redox-Regulated Transcription Factor SoxR †
  57. In vivo kinetics of a redox-regulated transcriptional switch
  58. In vivo kinetics of a redox-regulated transcriptional switch soxR containing [2Fe2S] cluster
  59. Redox signal transduction via iron-sulfur clusters in the SoxR transcription activator
  60. Cysteine-to-Alanine Replacements in the Escherichia Coli SoxR Protein and the Role of the [2Fe-2S] Centers in Transcriptional Activation
  61. Substitutions at position 146 of cytochrome b affect drastically the properties of heme bL and the Qo site of Rhodobacter capsulatus cytochrome bc1 complex
  62. Redox Signal Transduction: Mutations Shifting [2Fe-2S] Centers of the SoxR Sensor-Regulator to the Oxidized Form
  63. The Redox State of the [2Fe-2S] Clusters in SoxR Protein Regulates Its Activity as a Transcription Factor
  64. Glutathione-mediated destabilization in vitro of [2Fe-2S] centers in the SoxR regulatory protein.
  65. Ion Pair Formation between Basic Residues at 144 of the Cyt b Polypeptide and the Ubiquinones at the Qo Site of the Cyt bc1 Complex
  66. Tyrosine 147 of cytochrome b is required for efficient electron transfer at the ubihydroquinone oxidase site (Qo) of the cytochrome bc1 complex
  67. Ubiquinone Pair in the Qo Site Central to the Primary Energy Conversion Reactions of Cytochrome bc1 Complex
  68. Hydroubiquinone-cytochrome c2 oxidoreductase from Rhodobacter capsulatus: Definition of a minimal, functional isolated preparation
  69. Cytochrome bc1 complex [2Fe-2S] cluster and its interaction with ubiquinone and ubihydroquinone at the Qo site: a double-occupancy Qo site model