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Multiple Orientations in a Physiological Complex: The Pyruvate-Ferredoxin Oxidoreductase−Ferredoxin System

https://doi.org/10.1021/bi0485878
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Outgoing claims: the papers this work cites, builds on, or argues with.

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Rapid kinetic studies of the electron-exchange reaction between cytochrome c3 and ferredoxin from Desulfovibrio desulfuricans Norway strain and their individual reactions with dithionite
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Comparative studies of two ferredoxins from Desulfovibrio desulfuricans Norway
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Chemical study of two flavodoxins extracted from sulfate reducing bacteria
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Refined crystal structure of ferredoxin II from Desulfovibrio gigas at 1·7 Å
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Permselective-membrane pyrolytic graphite electrode for the study of microvolumes of [2Fe-2S] ferredoxin
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Spectroscopic characterization of ferredoxins I and II from Desulfovibrio africanus
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Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus
inferredcites →https://doi.org/10.1016/0300-9084(96)88170-3openalex-snapshot
Structure-function relationships in the ferredoxin/ferredoxin: NADP+ reductase system from Anabaena
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Electrochemical study of flavin mononucleotide and of flavodoxin from desulfovibrio vulgaris hildenborough
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The cytochrome c3–[Fe]‐hydrogenase electron‐transfer complex: structural model by NMR restrained docking
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Site-specific mutations in human ferredoxin that affect binding to ferredoxin reductase and cytochrome P450scc.
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Clostridial pyruvate oxidoreductase and the pyruvate-oxidizing enzyme specific to nitrogen fixation in Klebsiella pneumoniae are similar enzymes.
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The Preparation and Enzymatic Hydrolysis of Reduced and S-Carboxymethylated Proteins
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Electron Carriers for the Phosphoroclastic Reaction of Desulfovibrio desulfuricans
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Isolation and Characteristics of Flavodoxin from Nitrogen-fixing Clostridium pasteurianum
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Some Factors in the Interpretation of Protein Denaturation
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[59] Purification of electron-transfer components from sulfate-reducing bacteria
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Investigation of the role of surface residues in the ferredoxin from Clostridium pasteurianum
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Protein-protein interaction in electron transfer reactions: The ferrodoxin/flavodoxin/ferredoxin:NADP+ reductase system from Anabaena
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Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
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Probing the Role of Electrostatic Forces in the Interaction of Clostridium pasteurianum Ferredoxin with Its Redox Partners
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Crystal structure of an electron-transfer complex between methylamine dehydrogenase and amicyanin
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Crystal Structure of the Ferredoxin I from Desulfovibrio africanus at 2.3-.ANG. Resolution
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A Hyperthermophilic Plant-Type [2Fe-2S] Ferredoxin from Aquifex aeolicus Is Stabilized by a Disulfide Bond
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Myoglobin and Cytochrome b5: A Nuclear Magnetic Resonance Study of a Highly Dynamic Protein Complex
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Plastocyanin−Cytochrome f Interactions: The Influence of Hydrophobic Patch Mutations Studied by NMR Spectroscopy
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The Electron Transfer Complexes of Cytochrome c Peroxidase from Paracoccus denitrificans
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Identification by NMR of the Binding Surface for the Histidine-Containing Phosphocarrier Protein HPr on the N-Terminal Domain of Enzyme I of the Escherichia coli Phosphotransferase System
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The δ-Subunit of Pyruvate Ferredoxin Oxidoreductase from Pyrococcus furiosus Is a Redox-Active, Iron−Sulfur Protein: Evidence for an Ancestral Relationship with 8Fe-Type Ferredoxins
inferredcites →https://doi.org/10.1021/bi992306sopenalex-snapshot
Heteronuclear NMR and Soft Docking: An Experimental Approach for a Structural Model of the Cytochrome c553−Ferredoxin Complex
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
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Principles of protein–protein recognition
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Nature of biological electron transfer
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Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.
inferredcites →https://doi.org/10.1042/bj1680205openalex-snapshot
Midpoint redox potentials of plant and algal ferredoxins
inferredcites →https://doi.org/10.1073/pnas.55.4.928openalex-snapshot
A new ferredoxin-dependent carbon reduction cycle in a photosynthetic bacterium.
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Structural Model of the Fe-Hydrogenase/Cytochromec 553 Complex Combining Transverse Relaxation-optimized Spectroscopy Experiments and Soft Docking Calculations
inferredcites →https://doi.org/10.1093/embo-reports/kvd057openalex-snapshot
A redox‐dependent interaction between two electron‐transfer partners involved in photosynthesis
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Hyperproduction of Recombinant Ferredoxins in Escherichia coli by Coexpression of the ORF1-ORF2-iscS-iscU-iscA-hscB-hscA-fdx-ORF3 Gene Cluster
inferredcites →https://doi.org/10.1110/ps.07501openalex-snapshot
A novel approach for assesing macromolecular complexes combining soft‐docking calculations with NMR data
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Structures and Functions of Four Anabolic 2‐Oxoacid Oxidoreductases in Methanobacterium Thermoautotrophicum
inferredcites →https://doi.org/10.1126/science.1334573openalex-snapshot
Crystal Structure of a Complex Between Electron Transfer Partners, Cytochrome c Peroxidase and Cytochrome c
inferredcites →https://doi.org/10.1128/jb.179.18.5684-5692.1997openalex-snapshot
Isolation and analysis of the gene encoding the pyruvate-ferredoxin oxidoreductase of Desulfovibrio africanus, production of the recombinant enzyme in Escherichia coli, and effect of carboxy-terminal deletions on its stability
inferredcites →https://doi.org/10.2210/pdb1frh/pdbopenalex-snapshot
AZOTOBACTER VINELANDII FERREDOXIN I: ALTERATION OF INDIVIDUAL SURFACE CHARGES AND THE [4FE-4S] CLUSTER REDUCTION POTENTIAL
inferredcites →https://doi.org/10.5860/choice.26-3877openalex-snapshot
Biology of anaerobic microorganisms
inferredcites →https://doi.org/10.5860/choice.34-3868openalex-snapshot
Protein electron transfer

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.2139/ssrn.4857463openalex-extracted
The Redox Landscape of the 2-Oxoacid:Ferredoxin Oxidoreductase Superfamily Reveals Universally Conserved Fe–S Cluster Potentials
inferred← citeshttps://doi.org/10.1002/0470028637.met220openalex-snapshot
Pyruvate–Ferredoxin Oxidoreductase
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc0647openalex-snapshot
Pyruvate–Ferredoxin Oxidoreductase
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Global transcriptome analysis of the tetrachloroethene-dechlorinating bacterium Desulfitobacterium hafniense Y51 in the presence of various electron donors and terminal electron acceptors
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Designing a modified clostridial 2[4Fe–4S] ferredoxin as a redox coupler to directly link photosystem I with a Pt nanoparticle
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The Catalytic Bias of 2-Oxoacid:ferredoxin Oxidoreductase in CO2: evolution and reduction through a ferredoxin-mediated electrocatalytic assay
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The redox landscape of pyruvate:ferredoxin oxidoreductases reveals often conserved Fe–S cluster potentials
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The Type I / Type II Cytochrome c3 Complex: an Electron Transfer Link in the Hydrogen-Sulfate Reduction Pathway
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Octomeric pyruvate-ferredoxin oxidoreductase from Desulfovibrio vulgaris
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Maximizing (Electro)catalytic CO2 Reduction with a Ferredoxin-Based Reduction Potential Gradient
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Disulfide Bond-Dependent Mechanism of Protection against Oxidative Stress in Pyruvate-Ferredoxin Oxidoreductase of Anaerobic Desulfovibrio Bacteria
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Light-driven carbon−carbon bond formation via CO 2 reduction catalyzed by complexes of CdS nanorods and a 2-oxoacid oxidoreductase
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Chlamydomonas reinhardtii Chloroplasts Contain a Homodimeric Pyruvate:Ferredoxin Oxidoreductase That Functions with FDX1
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Isolation of a High-Affinity Functional Protein Complex between OmcA and MtrC: Two Outer Membrane Decaheme c -Type Cytochromes of Shewanella oneidensis MR-1
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Electron Transfer from Semiconductor Nanocrystals to Redox Enzymes
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Protein-Protein Interaction Inhibition (2P2I): Fewer and Fewer Undruggable Targets
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Carbon Fixation in the Chemolithoautotrophic Bacterium Aquifex aeolicus Involves Two Low-Potential Ferredoxins as Partners of the PFOR and OGOR Enzymes
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L'analyse des mécanismes d'action d'Hsp27 a mis en évidence TCTP comme nouvelle cible thérapeutique des cancers de la prostate résistants à la castration.
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