On the public citation graph

Crystal structures of archaeal 2-oxoacid:ferredoxin oxidoreductases from Sulfolobus tokodaii

0 signed · 86 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.

Claim with ORCID

Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.

See reference health

What this work says

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

inferredcites →https://doi.org/10.1006/bbrc.1996.1200openalex-snapshot

Molecular Cloning, Sequencing, and Heterologous Expression of a Novel Zinc-Containing Ferredoxin Gene from a Thermoacidophilic ArchaeonSulfolobusSp. Strain 7

inferredcites →https://doi.org/10.1006/bbrc.2001.4542openalex-snapshot

The Genes for Anabolic 2-Oxoglutarate: Ferredoxin Oxidoreductase from Hydrogenobacter thermophilus TK-6

inferredcites →https://doi.org/10.1007/bfb0031008openalex-snapshot

The mammalian pyruvate dehydrogenase complex: Structure and regulation

inferredcites →https://doi.org/10.1007/s00792-013-0601-1openalex-snapshot

Sulfolobus tokodaii ST2133 is characterized as a thioredoxin reductase-like ferredoxin:NADP+ oxidoreductase

inferredcites →https://doi.org/10.1016/0014-5793(80)80236-5openalex-snapshot

A stable free radical intermediate in the reaction of 2‐oxoacid:ferredoxin oxidoreductases of Halobacterium halobium

inferredcites →https://doi.org/10.1016/0167-4838(93)90190-3openalex-snapshot

Purification and characterization of pyruvate ferredoxin oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus

inferredcites →https://doi.org/10.1016/0167-4838(95)00029-topenalex-snapshot

Isolation and characterization of the pyruvate-ferredoxin oxidoreductase from the sulfate-reducing bacterium Desulfovibrio africanus

inferredcites →https://doi.org/10.1016/0968-0004(82)90118-9openalex-snapshot

Pyruvate : ferredoxin oxidoreductase — new findings on an ancient enzyme

inferredcites →https://doi.org/10.1016/0969-2126(93)90025-copenalex-snapshot

A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase

inferredcites →https://doi.org/10.1016/j.bbapap.2008.10.006openalex-snapshot

Identification of the lysine residue responsible for coenzyme A binding in the heterodimeric 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus tokodaii, a thermoacidophilic archaeon, using 4-fluoro-7-nitrobenzofurazan as an affinity label

inferredcites →https://doi.org/10.1016/j.bbapap.2011.11.010openalex-snapshot

Radical reactions of thiamin pyrophosphate in 2-oxoacid oxidoreductases

inferredcites →https://doi.org/10.1016/j.bbapap.2014.01.015openalex-snapshot

Four Cys residues in heterodimeric 2-oxoacid:ferredoxin oxidoreductase are required for CoA-dependent oxidative decarboxylation but not for a non-oxidative decarboxylation

inferredcites →https://doi.org/10.1016/j.bbrc.2003.11.078openalex-snapshot

Characterization of two different 2-oxoglutarate:ferredoxin oxidoreductases from Hydrogenobacter thermophilus TK-6

inferredcites →https://doi.org/10.1016/j.febslet.2004.11.117openalex-snapshot

Gene expression and characterization of two 2‐oxoacid:ferredoxin oxidoreductases from Aeropyrum pernix K1

inferredcites →https://doi.org/10.1016/j.str.2005.10.013openalex-snapshot

Flexibility of Thiamine Diphosphate Revealed by Kinetic Crystallographic Studies of the Reaction of Pyruvate-Ferredoxin Oxidoreductase with Pyruvate

inferredcites →https://doi.org/10.1016/j.str.2006.10.004openalex-snapshot

Electron Transfer Complex Formation between Oxygenase and Ferredoxin Components in Rieske Nonheme Iron Oxygenase System

inferredcites →https://doi.org/10.1016/s0021-9258(18)43899-9openalex-snapshot

Functional and evolutionary implications of a [3Fe-4S] cluster of the dicluster-type ferredoxin from the thermoacidophilic archaeon, Sulfolobus sp. strain 7.

inferredcites →https://doi.org/10.1016/s0076-6879(97)76066-xopenalex-snapshot

[20] Processing of X-ray diffraction data collected in oscillation mode

inferredcites →https://doi.org/10.1016/s0162-0134(01)00410-xopenalex-snapshot

Zinc-coordination of aspartic acid-76 in Sulfolobus ferredoxin is not required for thermal stability of the molecule

inferredcites →https://doi.org/10.1016/s0167-4838(02)00280-7openalex-snapshot

Substrate recognition by 2-oxoacid:ferredoxin oxidoreductase from Sulfolobus sp. strain 7

inferredcites →https://doi.org/10.1016/s0959-440x(99)00027-5openalex-snapshot

Structure and electron transfer mechanism of pyruvate:ferredoxin oxidoreductase

inferredcites →https://doi.org/10.1021/acs.biochem.5b00521openalex-snapshot

The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism

inferredcites →https://doi.org/10.1021/bi0602516openalex-snapshot

EPR Spectroscopic and Computational Characterization of the Hydroxyethylidene-Thiamine Pyrophosphate Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase

inferredcites →https://doi.org/10.1021/bi061582lopenalex-snapshot

Direct Kinetic Evidence for Half-Of-The-Sites Reactivity in the E1 Component of the Human Pyruvate Dehydrogenase Multienzyme Complex through Alternating Sites Cofactor Activation

inferredcites →https://doi.org/10.1021/bi301591eopenalex-snapshot

Alternating Sites Reactivity Is a Common Feature of Thiamin Diphosphate-Dependent Enzymes As Evidenced by Isothermal Titration Calorimetry Studies of Substrate Binding

inferredcites →https://doi.org/10.1021/bi961966jopenalex-snapshot

The Crystal Structure of Zinc-Containing Ferredoxin from the Thermoacidophilic Archaeon Sulfolobus sp. Strain 7,

inferredcites →https://doi.org/10.1021/bi970403kopenalex-snapshot

Mechanism of the Clostridium thermoaceticum Pyruvate:Ferredoxin Oxidoreductase: Evidence for the Common Catalytic Intermediacy of the Hydroxyethylthiamine Pyropyrosphate Radical

inferredcites →https://doi.org/10.1021/cr020423eopenalex-snapshot

Pyruvate Ferredoxin Oxidoreductase and Its Radical Intermediate

inferredcites →https://doi.org/10.1021/ja01547a064openalex-snapshot

On the Mechanism of Thiamine Action. IV.1 Evidence from Studies on Model Systems

inferredcites →https://doi.org/10.1038/5870openalex-snapshot

Crystal structures of the key anaerobic enzyme pyruvate:ferredoxin oxidoreductase, free and in complex with pyruvate.

inferredcites →https://doi.org/10.1038/nchembio.62openalex-snapshot

Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes

inferredcites →https://doi.org/10.1038/nchembio788openalex-snapshot

The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography

inferredcites →https://doi.org/10.1038/nsb1096-834openalex-snapshot

Novel zinc-binding centre in thermoacidophilic archaeal ferredoxins

inferredcites →https://doi.org/10.1046/j.1432-1033.2001.02504.xopenalex-snapshot

Role of a highly conserved YPITP motif in 2‐oxoacid:ferredoxin oxidoreductase.

inferredcites →https://doi.org/10.1046/j.1432-1327.1999.00579.xopenalex-snapshot

Zinc and an N‐terminal extra stretch of the ferredoxin from a thermoacidophilic archaeon stabilize the molecule at high temperature

inferredcites →https://doi.org/10.1073/pnas.022510999openalex-snapshot

Snapshot of a key intermediate in enzymatic thiamin catalysis: Crystal structure of the α-carbanion of (α,β-dihydroxyethyl)-thiamin diphosphate in the active site of transketolase from Saccharomyces cerevisiae

inferredcites →https://doi.org/10.1073/pnas.1201280109openalex-snapshot

Unexpected tautomeric equilibria of the carbanion-enamine intermediate in pyruvate oxidase highlight unrecognized chemical versatility of thiamin

inferredcites →https://doi.org/10.1073/pnas.1518537113openalex-snapshot

One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography

inferredcites →https://doi.org/10.1093/dnares/8.4.123openalex-snapshot

Complete Genome Sequence of an Aerobic Thermoacidophilic Crenarchaeon, Sulfolobus tokodaii strain7

inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a021454openalex-snapshot

2-Oxoacid:Ferredoxin Oxidoreductase from the Thermoacidophilic Archaeon, Sulfolobus sp. Strain 7

inferredcites →https://doi.org/10.1093/oxfordjournals.molbev.a026218openalex-snapshot

A single eubacterial origin of eukaryotic pyruvate: ferredoxin oxidoreductase genes: implications for the evolution of anaerobic eukaryotes

inferredcites →https://doi.org/10.1107/97809553602060000865openalex-snapshot

PHENIX: a comprehensive Python-based system for macromolecular structure solution

inferredcites →https://doi.org/10.1107/s0021889813011461openalex-snapshot

RADDOSE-3D : time- and space-resolved modelling of dose in macromolecular crystallography

inferredcites →https://doi.org/10.1107/s0021889897006766openalex-snapshot

MOLREP : an Automated Program for Molecular Replacement

inferredcites →https://doi.org/10.1107/s0907444907035160openalex-snapshot

Photoreduction of the active site of the metalloprotein putidaredoxin by synchrotron radiation

inferredcites →https://doi.org/10.1107/s0907444909052925openalex-snapshot

PHENIX : a comprehensive Python-based system for macromolecular structure solution

inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot

Features and development of Coot

inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

inferredcites →https://doi.org/10.1111/j.1432-1033.1981.tb05376.xopenalex-snapshot

Purification and Properties of Two 2‐Oxoacid:Ferredoxin Oxidoreductases from Halobacterium halobium

inferredcites →https://doi.org/10.1111/j.1432-1033.1981.tb05377.xopenalex-snapshot

The Catalytic Mechanism of 2‐Oxoacid: Ferredoxin Oxidoreductases from Halobacterium halobium

inferredcites →https://doi.org/10.1111/j.1432-1033.1992.tb16792.xopenalex-snapshot

Improved purification, crystallization and primary structure of pyruvate:ferredoxin oxidoreductase from Halobacterium halobium

inferredcites →https://doi.org/10.1111/j.1742-4658.2009.06965.xopenalex-snapshot

Reaction mechanisms of thiamin diphosphate enzymes: new insights into the role of a conserved glutamate residue

inferredcites →https://doi.org/10.1111/j.1742-4658.2009.06966.xopenalex-snapshot

Reaction mechanisms of thiamin diphosphate enzymes: redox reactions

inferredcites →https://doi.org/10.1126/science.1066198openalex-snapshot

Crystal Structure of the Free Radical Intermediate of Pyruvate:Ferredoxin Oxidoreductase

inferredcites →https://doi.org/10.1126/science.1101030openalex-snapshot

A Molecular Switch and Proton Wire Synchronize the Active Sites in Thiamine Enzymes

inferredcites →https://doi.org/10.1126/science.275.5296.67openalex-snapshot

How Thiamine Diphosphate Is Activated in Enzymes

inferredcites →https://doi.org/10.1128/jb.178.1.248-257.1996openalex-snapshot

Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima

inferredcites →https://doi.org/10.1128/jb.178.11.3365-3368.1996openalex-snapshot

Purification and characterization of 2-oxoglutarate:ferredoxin oxidoreductase from a thermophilic, obligately chemolithoautotrophic bacterium, Hydrogenobacter thermophilus TK-6

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/10.1128/mmbr.69.3.393-425.2005openalex-snapshot

Posttranslational Protein Modification inArchaea

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/advs.75061openalex-snapshot

Enzymatic Basis for the Oxidative Branch of Aromatic Amino Acid Fermentation Leading to p ‐cresol Formation

inferred← citeshttps://doi.org/10.1007/s10989-020-10076-wopenalex-snapshot

Delineating Novel Therapeutic Drug and Vaccine Targets for Staphylococcus cornubiensis NW1T Through Computational Analysis

inferred← citeshttps://doi.org/10.1016/j.bbapap.2017.08.003openalex-snapshot

Determinants of thermostability in the cytochrome P450 fold

inferred← citeshttps://doi.org/10.1016/j.ccr.2016.10.003openalex-snapshot

The competition between chemistry and biology in assembling iron–sulfur derivatives. Molecular structures and electrochemistry. Part V. { [ Fe 4 S 4 ] ( S Cys γ ) 4 } proteins

inferred← citeshttps://doi.org/10.1016/j.gce.2025.06.006openalex-snapshot

Sustainable hybrid photo/electro-enzyme systems for CO2 conversion

inferred← citeshttps://doi.org/10.1016/j.ica.2016.09.028openalex-snapshot

The competition between chemistry and biology in assembling iron-sulfur derivatives. Molecular structures and electrochemistry. Part IV. {[Fe3S4](SγCys)3} proteins

inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.10.045openalex-snapshot

Important amino acid residues involved in folding and binding of protein–protein complexes

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/10.1016/j.joule.2018.12.006openalex-snapshot

A Reverse TCA Cycle 2-Oxoacid:Ferredoxin Oxidoreductase that Makes C-C Bonds from CO2

inferred← citeshttps://doi.org/10.1016/j.jphotobiol.2025.113305openalex-snapshot

A novel 450 nm blue laser-mediated sinoporphyrin sodium-based photodynamic therapy inactivates Cutibacterium acnes through stress-mediated metabolic alterations

inferred← citeshttps://doi.org/10.1016/j.str.2024.08.011openalex-snapshot

Structural organization of pyruvate: ferredoxin oxidoreductase from the methanogenic archaeon Methanosarcina acetivorans

inferred← citeshttps://doi.org/10.1073/pnas.1722329115openalex-snapshot

Binding site for coenzyme A revealed in the structure of pyruvate:ferredoxin oxidoreductase from Moorella thermoacetica

inferred← citeshttps://doi.org/10.1093/femsre/fuaa063openalex-snapshot

The biology of thermoacidophilic archaea from the order Sulfolobales

inferred← citeshttps://doi.org/10.1101/2025.11.27.691053openalex-snapshot

Unraveling the archaeal virosphere: diversity, functional and virus-host interactions

inferred← citeshttps://doi.org/10.1111/febs.14105openalex-snapshot

Oxidative Stickland reactions in an obligate aerobic organism – amino acid catabolism in the Crenarchaeon Sulfolobus solfataricus

inferred← citeshttps://doi.org/10.1111/febs.14981openalex-snapshot

New light on ancient enzymes – in vitro CO 2 Fixation by Pyruvate Synthase of Desulfovibrio africanus and Sulfolobus acidocaldarius

inferred← citeshttps://doi.org/10.1128/aem.01451-23openalex-snapshot

Metaproteomics analysis of anaerobic digestion of food waste by the addition of calcium peroxide and magnetite

inferred← citeshttps://doi.org/10.1128/aem.02223-18openalex-snapshot

Metabolites Involved in Aerobic Degradation of the A and B Rings of Estrogen

inferred← citeshttps://doi.org/10.1186/s40168-023-01728-2openalex-snapshot

Metagenomic characterization of a novel non-ammonia-oxidizing Thaumarchaeota from hadal sediment

inferred← citeshttps://doi.org/10.3390/biology11081247openalex-snapshot

Thermostable and O2-Insensitive Pyruvate Decarboxylases from Thermoacidophilic Archaea Catalyzing the Production of Acetaldehyde

inferred← citeshttps://doi.org/10.3390/biology12010059openalex-snapshot

Photoautotrophic Growth Rate Enhancement of Synechocystis sp. PCC6803 by Heterologous Production of 2-Oxoglutarate:Ferredoxin Oxidoreductase from Chlorobaculum tepidum

inferred← citeshttps://doi.org/10.3390/catal12040399openalex-snapshot

Promotion of Carbon Dioxide Biofixation through Metabolic and Enzyme Engineering

inferred← citeshttps://doi.org/10.3390/life7040039openalex-snapshot

Origin of the Reductive Tricarboxylic Acid (rTCA) Cycle-Type CO2 Fixation: A Perspective

inferred← citeshttps://doi.org/10.5772/intechopen.72164openalex-snapshot

B Group Vitamins - Current Uses and Perspectives

inferred← citeshttps://doi.org/10.5772/intechopen.77170openalex-snapshot

Vitamin B1 (Thiamine) Metabolism and Regulation in Archaea

Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.