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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