DIRECT ELECTROCHEMISTRY IN THE CHARACTERIZATION OF REDOX PROTEINS - NOVEL PROPERTIES OF AZOTOBACTER 7FE FERREDOXIN

DIRECT ELECTROCHEMISTRY IN THE CHARACTERIZATION OF REDOX PROTEINS - NOVEL PROPERTIES OF AZOTOBACTER 7FE FERREDOXIN

Fast diffusion-dominated electron transfer between Azotobacter chroococcum 7Fe ferredoxin, FdI, and pyrolytic graphite 'edge' electrodes, promoted by aminoglycosides, permits detailed voltammetric studies and preparation of oxidation states inaccessible by chemical titration. The [3Fe-4S]...

Deskribapen osoa

Xehetasun bibliografikoak
Egile Nagusiak:	Armstrong, F, George, S, Thomson, A, Yates, M
Formatua:	Journal article
Hizkuntza:	English
Argitaratua:	1988

Antzeko izenburuak

REDOX PROPERTIES OF AZOTOBACTER FE-7 FERREDOXIN
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Mechanisms of redox-coupled proton transfer in proteins: role of the proximal proline in reactions of the [3Fe-4S] cluster in Azotobacter vinelandii ferredoxin I.
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DIRECT ELECTROCHEMISTRY OF REDOX PROTEINS
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Alteration of the reduction potential of the [4Fe-4S] (2+/+) cluster of azotobacter vinelandii ferredoxin I
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Site-directed mutagenesis of Azotobacter vinelandii ferredoxin I. Changes in [4Fe-4S] cluster reduction potential and reactivity.
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Alteration of the reduction potential of the [4Fe-4S](2+/+) cluster of Azotobacter vinelandii ferredoxin I.
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Electrochemical and spectroscopic characterization of the 7Fe form of ferredoxin III from Desulfovibrio africanus.
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Alteration of the reduction potential of the [4Fe-4S](2+) cluster of Azotobacter vinelandii ferredoxin I
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Protein film cryovoltammetry - demonstration with a 7Fe ferredoxin
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Azotobacter vinelandii ferredoxin I. Aspartate 15 facilitates proton transfer to the reduced [3Fe-4S] cluster.
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DIRECT ELECTROCHEMISTRY OF REDOX PROTEINS AT PYROLYTIC-GRAPHITE ELECTRODES
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VOLTAMMETRIC STUDY OF PROTON-GATED ELECTRON-TRANSFER IN A MUTANT FERREDOXIN - ALTERING ASPARTATE TO ASPARAGINE BLOCKS OXIDATION OF THE [3FE-4S] CLUSTER OF AZOTOBACTER-VINELANDII FERREDOXIN-I
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Novel redox chemistry of [3Fe-4S] clusters: Electrochemical characterization of the all-Fe(II) form of the [3Fe-4S] cluster generated reversibly in various proteins and its spectroscopic investigation in Sulfolobus acidocaldarius ferredoxin
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ELECTROCHEMICAL AND SPECTROSCOPIC STUDIES OF FERREDOXINS
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Azotobacter vinelandii ferredoxin I. Alteration of individual surface charges and the [4FE-4S]2+/+ cluster reduction potential.
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Discovery of a novel ferredoxin from Azotobacter vinelandii containing two [4Fe-4S] clusters with widely differing and very negative reduction potentials.
nork: Gao-Sheridan, H, et al.
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Protein film cryovoltammetry: demonstrations with a 7Fe ([3Fe-4S]+[4Fe-4S]) ferredoxin
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Azotobacter vinelandii ferredoxin I: a sequence and structure comparison approach to alteration of [4Fe-4S]2+/+ reduction potential.
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Y13C Azotobacter vinelandii ferredoxin I. A designed [Fe-S] ligand motif contains a cysteine persulfide.
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Electrochemical and spectroscopic characterization of the conversion of the 7Fe into the 8Fe form of ferredoxin III from Desulfovibrio africanus. Identification of a [4Fe-4S] cluster with one non-cysteine ligand.
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A T14C variant of Azotobacter vinelandii ferredoxin I undergoes facile [3Fe-4S]0 to [4Fe-4S]2+ conversion in vitro but not in vivo.
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SURFACE SELECTIVITY IN THE DIRECT ELECTROCHEMISTRY OF REDOX PROTEINS - CONTRASTING BEHAVIOR AT EDGE AND BASAL PLANES OF GRAPHITE
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At 14/ΔD15 Azotobacter vinelandii ferredoxin I: Creation of a new CysXXCysXXCys motif that ligates a [4Fe-4S] cluster
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Delta T 14/Delta D 15 Azotobacter vinelandii ferredoxin I: creation of a new CysXXCysXXCys motif that ligates a [4Fe-4S] cluster.
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Investigations of the oxidative disassembly of Fe-S clusters in Clostridium pasteurianum 8Fe ferredoxin using pulsed-protein-film voltammetry.
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DIRECT ELECTROCHEMICAL REDUCTION OF FERREDOXIN PROMOTED BY MG-2+
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DIRECT ELECTROCHEMISTRY OF THE BLUE COPPER PROTEIN PLASTOCYANIN
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INVESTIGATION OF METAL-ION UPTAKE REACTIVITIES OF [3FE-4S] CLUSTERS IN PROTEINS - VOLTAMMETRY OF COADSORBED FERREDOXIN AMINOCYCLITOL FILMS AT GRAPHITE-ELECTRODES AND SPECTROSCOPIC IDENTIFICATION OF TRANSFORMED CLUSTERS
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Voltammetric studies of the reactions of iron-sulphur clusters ([3Fe-4S] or [M3Fe-4S]) formed in Pyrococcus furiosus ferredoxin.
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VOLTAMMETRIC CHARACTERIZATION OF RAPID AND REVERSIBLE BINDING OF AN EXOGENOUS THIOLATE LIGAND AT A [4FE-4S] CLUSTER IN FERREDOXIN-III FROM DESULFOVIBRIO-AFRICANUS
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Ferredoxin III of Desulfovibrio africanus: sequencing of the native gene and characterization of a histidine-tagged form.
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Crystal structures of ferredoxin variants exhibiting large changes in [Fe-S] reduction potential.
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Unusual spectroscopic and electrochemical properties of the 2[4Fe-4S] ferredoxin of Thauera aromatica.
nork: Boll, M, et al.
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[3Fe-4S] <--> [4Fe-4S] cluster interconversion in Desulfovibrio africanus ferredoxin III: properties of an Asp14 --> Cys mutant.
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EVIDENCE FOR REVERSIBLE MULTIPLE REDOX TRANSFORMATIONS OF [3FE-4S] CLUSTERS
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DYNAMIC ELECTROCHEMISTRY OF IRON-SULFUR PROTEINS
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Electrochemistry of immobilised redox droplets: Concepts and applications
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BINDING OF THALLIUM(I) TO A [3FE-4S] CLUSTER - EVIDENCE FOR RAPID AND REVERSIBLE FORMATION OF [TL3FE-4S]2+ AND [TL3FE-4S]1+ CENTERS IN A FERREDOXIN
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KINETIC STUDIES ON REACTIONS OF IRON-SULFUR PROTEINS .2. EXTENSION OF THE RANGE OF OXIDANTS IN THE REACTION OF REDUCED PARSLEY 2-FE FERREDOXIN AND IDENTIFICATION OF SPECIFIC BINDING-SITES USING REDOX INACTIVE CR(NH3)63+( AND CR(EN)33+)
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Reversible electrochemistry of fumarate reductase immobilized on an electrode surface. Direct voltammetric observations of redox centers and their participation in rapid catalytic electron transport.
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