Characterization of [4Fe-4Se]2+/3+ high-potential iron-sulfur protein from Chromatium vinosum (original) (raw)
Oxidation-reduction properties of Chromatium vinosum high potential iron-sulfur protein
Isaac Mizrahi
Biochemistry, 1976
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Investigation of the Reduced High-Potential Iron−Sulfur Protein from Chromatium vinosum and Relevant Model Compounds: A Unified Picture of the Electronic Structure of [Fe4S4]2+ Systems through Magnetic and Optical Studies
Jeanne Jordanov
Inorganic Chemistry, 2003
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Intramolecular electron transfer in [4Fe-4S] proteins: estimates of the reorganization energy and electronic coupling in Chromatium vinosum ferredoxin
Jean-marc Moulis
JBIC Journal of Biological Inorganic Chemistry, 2001
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Comparison and characterization of the [Fe 4 S 4 ] 2+/3+ centre in the wild-type and C77S mutated HiPIPs from Chromatium vinosum monitored by Mössbauer, 57 Fe ENDOR and EPR spectroscopies
Andreas Dilg
Journal of Biological Inorganic Chemistry, 2001
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Electron paramagnetic resonance and optical evidence for interaction between siroheme and the tetranuclear iron-sulfur center (Fe4S4) prosthetic groups in complexes of Escherichia coli sulfite reductase hemoprotein with added ligands
Lewis Siegel
Biochemistry, 1983
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Factors Influencing Redox Thermodynamics and Electron Self-Exchange for the [Fe4S4] Cluster in Chromatium vinosum High Potential Iron Protein: The Role of Core Aromatic Residues in Defining Cluster Redox Chemistry
Anshu Agarwal
Biochemistry, 1996
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Redox chemistry of the Schizosaccharomyces pombe ferredoxin electron-transfer domain and influence of Cys to Ser substitutions
Sheref Mansy
Journal of Inorganic Biochemistry, 2011
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Site-specific oxidation of the [Fe4S4] cubanes in high-potential iron sulfur proteins as probed by EPR and orientation-selective proton ENDOR spectroscopy:Ectothiorhodospira halophila I versusRhodocyclus tenuis
Reinhard Kappl
Applied Magnetic Resonance, 2007
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Oxidation state dependence of proton exchange near the iron-sulfur centers in ferredoxins and high-potential iron-sulfur proteins
Jack Peisach
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
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Structural origins of redox potentials in Fe-S proteins: electrostatic potentials of crystal structures
Toshiko Ichiye
Biophysical Journal, 1996
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Crystal Structure and Stability Studies of C77S HiPIP: A Serine Ligated [4Fe-4S] Cluster †
Sheref Mansy
Biochemistry, 2002
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Structure of Rhodoferax fermentans high-potential iron–sulfur protein solved by MAD
Ana Gonzalez
Acta Crystallographica Section D Biological Crystallography, 2003
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The role of a conserved tyrosine residue in high-potential iron sulfur proteins
I. Felli
Protein Science, 1995
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Iron-Sulfur Cluster Cysteine-to-Serine Mutants of Anabaena [2Fe-2S] Ferredoxin Exhibit Unexpected Redox Properties and Are Competent in Electron Transfer to Ferredoxin:NADP+ Reductase
John Hurley
Biochemistry, 1997
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Electron transfer in iron(II)iron(III) model complexes of iron-oxo proteins
David Hendrickson
Journal of the American Chemical Society, 1992
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Direct Resonance Raman Evidence for a Trans Influence on the Ferryl Fragment in Models of Compound I Intermediates of Heme Enzymes
Zeev Gross
Journal of the American Chemical Society, 1996
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The iron-sulfur cluster in the oxidized high-potential iron protein from Ectothiorhodospira halophila
Stefano Ciurli
Journal of the …, 1993
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Hyperfine-Shifted 13 C Resonance Assignments in an Iron−Sulfur Protein with Quantum Chemical Verification: Aliphatic C−H···S 3-Center−4-Electron Interactions
John Markley
Journal of the American Chemical Society, 2011
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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
Lewis Siegel
Biochemistry, 1997
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Sequence Determination of Reduction Potentials by Cysteinyl Hydrogen Bonds and Peptide Dipoles in [4Fe4S] Ferredoxins
Toshiko Ichiye
Biophysical Journal, 2001
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A Structural Model of a P450-Ferredoxin Complex from Orientation-Selective Double ElectronElectron Resonance Spectroscopy
Alice Bowen
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The environment of Fe4S4 clusters in ferredoxins and high-potential iron proteins. New information from x-ray crystallography and resonance Raman spectroscopy
Gabriele Backes
J Am Chem Soc, 1991
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J. Biol. Chem.-2011-Liu.pdf
Qian Du
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Resonance Raman spectroscopic evidence for a common [3-iron-4-sulfur] structure among proteins containing three-iron centers
Thomas Spiro
Journal of the American Chemical Society, 1983
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Modulation of the Redox Potential of the [Fe(SCys) 4 ] Site in Rubredoxin by the Orientation of a Peptide Dipole
Toshiko Ichiye
Biochemistry, 1999
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Synthetic analogs of the active sites of iron-sulfur proteins. VIII. Some electronic properties of [Fe4S4(SR)4]3; analogs of reduced bacterial ferredoxins
Lawrence Que
Biochemical and Biophysical Research Communications, 1974
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Spectroscopic Characterization of Site-Specific [Fe4S4] Cluster Chemistry in Ferredoxin:Thioredoxin Reductase: Implications for the Catalytic Mechanism
Elizabeth Walters
Journal of the American Chemical Society, 2005
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Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes
Lewis Siegel
Biochemistry, 1989
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The Loop Region Covering the Iron-Sulfur Cluster in Bovine Adrenodoxin Comprises a New Interaction Site for Redox Partners
Rita Bernhardt
Journal of Biological Chemistry, 2000
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Protein-protein interaction in electron transfer reactions: The ferrodoxin/flavodoxin/ferredoxin:NADP+ reductase system from Anabaena
Milagros Medina
Biochimie, 1998
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A theoretical multiscale treatment of protein–protein electron transfer: The ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems
Israel Vaca
Biochimica et Biophysica Acta (BBA) - Bioenergetics, 2015
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S Kedge XAS and DFT Calculations on Cytochrome P450: Covalent and Ionic Contributions to the Cysteine-Fe Bond and Their Contribution to Reactivity
Abhishek Dey
Journal of The American Chemical Society, 2009
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