All Stories

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