Iron-Sulfur Proteins

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  Subject Areas on Research

  • An active site tyrosine influences the ability of the dimethyl sulfoxide reductase family of molybdopterin enzymes to reduce S-oxides. 
  • Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation. 
  • Biallelic mutations in FDXR cause neurodegeneration associated with inflammation. 
  • Characterisation of PduS, the pdu metabolosome corrin reductase, and evidence of substructural organisation within the bacterial microcompartment. 
  • Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe. 
  • Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase. 
  • Confirmation of the involvement of protein domain movement during the catalytic cycle of the cytochrome bc1 complex by the formation of an intersubunit disulfide bond between cytochrome b and the iron-sulfur protein. 
  • Construction of a novel redox protein by rational design: conversion of a disulfide bridge into a mononuclear iron-sulfur center. 
  • Crystal structure of DMSO reductase: redox-linked changes in molybdopterin coordination. 
  • Effect of famoxadone on photoinduced electron transfer between the iron-sulfur center and cytochrome c1 in the cytochrome bc1 complex. 
  • Electron paramagnetic resonance and optical spectroscopic evidence for interaction between siroheme and Fe4S4 prosthetic groups in Escherichia coli sulfite reductase hemoprotein subunit. 
  • Electron paramagnetic resonance properties and oxidation-reduction potentials of the molybdenum, flavin, and iron-sulfur centers of chicken liver xanthine dehydrogenase. 
  • Elucidation of a [4Fe-4S] cluster degradation pathway: rapid kinetic studies of the degradation of Chromatium vinosum HiPIP. 
  • Evidence for the intertwined dimer of the cytochrome bc(1) complex in solution. 
  • Formate dehydrogenase from Methanobacterium formicicum. Electron paramagnetic resonance spectroscopy of the molybdenum and iron-sulfur centers. 
  • Hydrogen sulphide enhances photosynthesis through promoting chloroplast biogenesis, photosynthetic enzyme expression, and thiol redox modification in Spinacia oleracea seedlings. 
  • Identification of the iron-sulfur center of spinach ferredoxin-nitrite reductase as a tetranuclear center, and preliminary EPR studies of mechanism. 
  • Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum. 
  • Inter- and intra-molecular electron transfer in the cytochrome bc(1) complex. 
  • Iron and copper in mitochondrial diseases. 
  • Iron-dependent regulation of the divalent metal ion transporter. 
  • Isolation of the domain containing the molybdenum, iron-sulfur I, and iron-sulfur II centers of chicken liver xanthine dehydrogenase. 
  • Mechanism of assembly of the Bis(Molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase. 
  • Molecular cloning of dimethyl sulfoxide reductase from Rhodobacter sphaeroides. 
  • Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans. 
  • Mössbauer evidence for exchange-coupled siroheme and [4Fe-4S] prosthetic groups in Escherichia coli sulfite reductase. Studies of the reduced states and of a nitrite turnover complex. 
  • Mössbauer spectroscopic studies of Escherichia coli sulfite reductase. Evidence for coupling between the siroheme and Fe4S4 cluster prosthetic groups. 
  • Mössbauer studies of Escherichia coli sulfite reductase complexes with carbon monoxide and cyanide. Exchange coupling and intrinsic properties of the [4Fe-4S] cluster. 
  • Optical and electron paramagnetic resonance spectroscopic studies on purine hydroxylase II from Aspergillus nidulans. 
  • Photoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force. 
  • Protein electron transfer rates set by the bridging secondary and tertiary structure. 
  • Pulsed EPR studies of the exchangeable proton at the molybdenum center of dimethyl sulfoxide reductase. 
  • Re-design of Rhodobacter sphaeroides dimethyl sulfoxide reductase. Enhancement of adenosine N1-oxide reductase activity. 
  • Resonance Raman characterization of biotin sulfoxide reductase. Comparing oxomolybdenum enzymes in the ME(2)SO reductase family. 
  • Resonance Raman spectroscopic characterization of the molybdopterin active site of DMSO reductase. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes. 
  • Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes. 
  • Spectroscopic studies of the molybdenum-containing dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans. 
  • Structural basis of multifunctional bovine mitochondrial cytochrome bc1 complex. 
  • Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. 
  • The construction of metal centers in proteins by rational design. 
  • The extra fragment of the iron-sulfur protein (residues 96-107) of Rhodobacter sphaeroides cytochrome bc1 complex is required for protein stability. 
  • The fidelity of DNA replication, particularly on GC-rich templates, is reduced by defects of the Fe-S cluster in DNA polymerase δ. 
  • The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase. 
  • The rational design and construction of a cuboidal iron-sulfur protein. 
  • The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.