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Redox potential changes during ATP‐dependent corrinoid reduction determined by redox titrations with europium(II)–DTPA

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/cbic.201402270openalex-snapshot
The Benzoyl‐Coenzyme A Reductase and 2‐Hydroxyacyl‐Coenzyme A Dehydratase Radical Enzyme Family
inferredcites →https://doi.org/10.1006/abio.1976.9999openalex-snapshot
A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye Binding
inferredcites →https://doi.org/10.1006/jmbi.2000.4496openalex-snapshot
Crystal structure of the Acidaminococcus fermentans 2-hydroxyglutaryl-CoA dehydratase component A
inferredcites →https://doi.org/10.1007/bf00871640openalex-snapshot
Metabolism of homoacetogens
inferredcites →https://doi.org/10.1007/s00203-005-0001-8openalex-snapshot
Veratrol-O-demethylase of Acetobacterium dehalogenans: ATP-dependent reduction of the corrinoid protein
inferredcites →https://doi.org/10.1007/s002030050479openalex-snapshot
Isolation of O -demethylase, an ether-cleaving enzyme system of the homoacetogenic strain MC
inferredcites →https://doi.org/10.1016/j.ccr.2015.11.001openalex-snapshot
Redox chemistry of cobalamin and its derivatives
inferredcites →https://doi.org/10.1021/bi00087a005openalex-snapshot
Assignment of enzymic function to specific protein regions of cobalamin-dependent methionine synthase from Escherichia coli
inferredcites →https://doi.org/10.1021/bi001645eopenalex-snapshot
MgATP-Bound and Nucleotide-Free Structures of a Nitrogenase Protein Complex between the Leu 127Δ-Fe-Protein and the MoFe-Protein,
inferredcites →https://doi.org/10.1021/bi00449a019openalex-snapshot
Spectroelectrochemical studies of the corrinoid/iron-sulfur protein involved in acetyl coenzyme A synthesis by Clostridium thermoaceticum
inferredcites →https://doi.org/10.1021/bi300571zopenalex-snapshot
On the ATP-Dependent Activation of the Radical Enzyme (R)-2-Hydroxyisocaproyl-CoA Dehydratase
inferredcites →https://doi.org/10.1021/bi800437gopenalex-snapshot
Reduction of the Iron−Sulfur Clusters in Mitochondrial NADH:Ubiquinone Oxidoreductase (Complex I) by EuII-DTPA, a Very Low Potential Reductant
inferredcites →https://doi.org/10.1021/ja00425a039openalex-snapshot
Electrochemistry of vitamin B12. I. Role of the base-on/base-off reaction in the oxidoreduction mechanism of the B12r-B12s system
inferredcites →https://doi.org/10.1021/ja1067178openalex-snapshot
Uncoupling Nitrogenase: Catalytic Reduction of Hydrazine to Ammonia by a MoFe Protein in the Absence of Fe Protein-ATP
inferredcites →https://doi.org/10.1023/a:1022525626986openalex-snapshot
Multiple Functions of Corrinoids in Prokaryote Biology
inferredcites →https://doi.org/10.1038/141896b0openalex-snapshot
Fermente, Hormone, Vitamine
inferredcites →https://doi.org/10.1038/ncomms5626openalex-snapshot
ATP-induced electron transfer by redox-selective partner recognition
inferredcites →https://doi.org/10.1039/b308188eopenalex-snapshot
Instantaneous, stoichiometric generation of powerfully reducing states of protein active sites using Eu(ii) and polyaminocarboxylate ligands
inferredcites →https://doi.org/10.1073/pnas.1117126109openalex-snapshot
Redox-dependent complex formation by an ATP-dependent activator of the corrinoid/iron-sulfur protein
inferredcites →https://doi.org/10.1073/pnas.241375598openalex-snapshot
Mechanism of ATP-driven electron transfer catalyzed by the benzene ring-reducing enzyme benzoyl- CoA reductase
inferredcites →https://doi.org/10.1073/pnas.56.3.979openalex-snapshot
The nitrogenase system from Azotobacter: two-enzyme requirement for N2 reduction, ATP-dependent H2 evolution, and ATP hydrolysis.
inferredcites →https://doi.org/10.1073/pnas.75.6.2699openalex-snapshot
Nitrogenase and nitrogenase reductase associate and dissociate with each catalytic cycle.
inferredcites →https://doi.org/10.1074/jbc.274.17.11513openalex-snapshot
The Role of an Iron-Sulfur Cluster in an Enzymatic Methylation Reaction
inferredcites →https://doi.org/10.1074/jbc.m117.801548openalex-snapshot
Unraveling the interactions of the physiological reductant flavodoxin with the different conformations of the Fe protein in the nitrogenase cycle
inferredcites →https://doi.org/10.1074/jbc.m807392200openalex-snapshot
RamA, a Protein Required for Reductive Activation of Corrinoid-dependent Methylamine Methyltransferase Reactions in Methanogenic Archaea
inferredcites →https://doi.org/10.1098/rsta.2004.1539openalex-snapshot
Structural basis of biological nitrogen fixation
inferredcites →https://doi.org/10.1111/j.1432-1033.1997.00840.xopenalex-snapshot
Benzoyl‐CoA Reductase (Dearomatizing), A Key Enzyme of Anaerobic Aromatic Metabolism
inferredcites →https://doi.org/10.1111/j.1742-4658.2004.04498.xopenalex-snapshot
2‐Hydroxyisocaproyl‐CoA dehydratase and its activator from Clostridium difficile
inferredcites →https://doi.org/10.1111/mmi.12582openalex-snapshot
Kinetic regulation of a corrinoid‐reducing metallo‐ ATPase by its substrates
inferredcites →https://doi.org/10.1126/science.1115653openalex-snapshot
Nitrogenase Complexes: Multiple Docking Sites for a Nucleotide Switch Protein
inferredcites →https://doi.org/10.1128/jb.01104-08openalex-snapshot
The Ether-Cleaving Methyltransferase System of the Strict Anaerobe Acetobacterium dehalogenans : Analysis and Expression of the Encoding Genes
inferredcites →https://doi.org/10.1146/annurev.biochem.78.070907.103812openalex-snapshot
Mechanism of Mo-Dependent Nitrogenase
inferredcites →https://doi.org/10.1146/annurev.mi.26.100172.001035openalex-snapshot
Ferredoxins and Flavodoxins of Bacteria

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/10.1002/9781119951438.eibc2870openalex-snapshot
Double Cubane Cluster Protein and Its Reductase
inferred← citeshttps://doi.org/10.1002/cctc.202500877openalex-snapshot
Cobalamin‐Dependent Aryl Methyl Ether O ‐Demethylases: Promising Enzymes for Biocatalytic Applications from Lignin Valorization to Organic Synthesis
inferred← citeshttps://doi.org/10.1016/j.bioelechem.2026.109233openalex-snapshot
Bioluminescence-based electrochemical sensor for dual-mode direct hydrocarbon detection in saline water utilizing Photobacterium leiognathi and d-luciferin-modified au-SPE
inferred← citeshttps://doi.org/10.1016/j.jbc.2025.110380openalex-snapshot
The redox landscape of pyruvate:ferredoxin oxidoreductases reveals often conserved Fe–S cluster potentials
inferred← citeshttps://doi.org/10.1021/acscatal.1c01038openalex-snapshot
ATP Binding and a Second Reduction Enables a Conformationally Gated Uphill Electron Transfer
inferred← citeshttps://doi.org/10.1038/s41586-025-08890-7openalex-snapshot
Structure of the ATP-driven methyl-coenzyme M reductase activation complex
inferred← citeshttps://doi.org/10.1073/pnas.2203576119openalex-snapshot
Structural basis for coupled ATP-driven electron transfer in the double-cubane cluster protein
inferred← citeshttps://doi.org/10.1093/femsle/fnaa128openalex-snapshot
Kinetic and substrate complex characterization of RamA, a corrinoid protein reductive activase from Methanosarcina barkeri
inferred← citeshttps://doi.org/10.1093/femsre/fuaa040openalex-snapshot
Methanol and methyl group conversion in acetogenic bacteria: biochemistry, physiology and application
inferred← citeshttps://doi.org/10.1111/1462-2920.15643openalex-snapshot
Biochemistry of methanol‐dependent acetogenesis in Eubacterium callanderi KIST612
inferred← citeshttps://doi.org/10.1111/febs.15290openalex-snapshot
Flavodoxin hydroquinone provides electrons for the ATP‐dependent reactivation of protein‐bound corrinoid cofactors
inferred← citeshttps://doi.org/10.1128/jb.00257-25openalex-snapshot
Overexpression of 2-mercaptoethanesulfonate biosynthesis genes comDE protects methane-producing archaea from oxidative stress
inferred← citeshttps://doi.org/10.1134/s0026261722603128openalex-snapshot
Transformation of Methoxylated Aromatic Compounds by Anaerobic Microorganisms
inferred← citeshttps://doi.org/10.21203/rs.3.rs-9327205/v1openalex-snapshot
Interaction of vitamin B12 with bromoform, other halogenated methane analogs, and Asparagopsis, on methanogenesis in mixed rumen cultures
inferred← citeshttps://doi.org/10.21248/gups.66881openalex-snapshot
Untersuchungen zur Physiologie und Energiekonservierung im acetogenen Bakterium Eubacterium callanderi KIST612
inferred← citeshttps://doi.org/10.31857/s0026365622600651openalex-snapshot
Transformation of Methoxylated Aromatic Compounds by Anaerobic Microorganisms
inferred← citeshttps://doi.org/10.3390/plants14152337openalex-snapshot
Plant Electrophysiological Parameters Represent Leaf Intracellular Water–Nutrient Metabolism and Immunoregulations in Brassica rapa During Plasmodiophora Infection
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