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Reaction Cycle of the Dissimilatory Sulfite Reductase from Archaeoglobus fulgidus,
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1007/0-306-48127-8_17openalex-snapshot
Ferredoxin and Ferredoxin-Dependent Enzymes
inferredcites →https://doi.org/10.1007/bf00276538openalex-snapshot
Formation of thiosulfate and trithionate during sulfite reduction by washed cells of Desulfovibrio desulfuricans
inferredcites →https://doi.org/10.1007/bf00871638openalex-snapshot
Metabolism of sulfate-reducing prokaryotes
inferredcites →https://doi.org/10.1016/0003-2697(85)90442-7openalex-snapshot
Measurement of protein using bicinchoninic acid
inferredcites →https://doi.org/10.1016/j.febslet.2005.07.029openalex-snapshot
X‐ray structure of the γ‐subunit of a dissimilatory sulfite reductase: Fixed and flexible C‐terminal arms
inferredcites →https://doi.org/10.1016/j.febslet.2005.07.044openalex-snapshot
Deletion of flavoredoxin gene in Desulfovibrio gigas reveals its participation in thiosulfate reduction
inferredcites →https://doi.org/10.1016/j.jmb.2008.04.027openalex-snapshot
Structure of the Dissimilatory Sulfite Reductase from the Hyperthermophilic Archaeon Archaeoglobus fulgidus
inferredcites →https://doi.org/10.1016/s0021-9258(18)94289-4openalex-snapshot
Methyl Viologen-linked Sulfite Reductase from Spinach Leaves
inferredcites →https://doi.org/10.1016/s0021-9258(19)42921-9openalex-snapshot
Reduced Nicotinamide Adenine Dinucleotide Phosphate-Sulfite Reductase of Enterobacteria
inferredcites →https://doi.org/10.1016/s0021-9258(19)43436-4openalex-snapshot
Siroheme and Sirohydrochlorin
inferredcites →https://doi.org/10.1016/s0021-9258(19)44469-4openalex-snapshot
Reduced Nicotinamide Adenine Dinucleotide Phosphate-Sulfite Reductase of Enterobacteria
inferredcites →https://doi.org/10.1016/s0021-9258(20)65147-xopenalex-snapshot
Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes.
inferredcites →https://doi.org/10.1016/s0022-328x(02)01715-1openalex-snapshot
Handbook of metalloproteins
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/s0959-440x(96)80003-0openalex-snapshot
The relationship between structure and function for the sulfite reductases
inferredcites →https://doi.org/10.1016/s0969-2126(03)00156-4openalex-snapshot
Crystal Structure of Dissimilatory Sulfite Reductase D (DsrD) Protein—Possible Interaction with B- and Z-DNA by Its Winged-Helix Motif
inferredcites →https://doi.org/10.1021/ac60030a028openalex-snapshot
Spectrophotometric Determination of Hydrogen Sulfide
inferredcites →https://doi.org/10.1021/ac60276a029openalex-snapshot
Cyanolysis and spectrophotometric estimation of trithionate in mixture with thiosulfate and tetrathionate
inferredcites →https://doi.org/10.1021/bi00439a023openalex-snapshot
Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 2. Fe4S4 cluster vibrational modes
inferredcites →https://doi.org/10.1021/bi050981yopenalex-snapshot
Structure of Spinach Nitrite Reductase: Implications for Multi-electron Reactions by the Iron−Sulfur:Siroheme Cofactor,
inferredcites →https://doi.org/10.1021/bi7021415openalex-snapshot
Binding and Reduction of Sulfite by Cytochrome c Nitrite Reductase,
inferredcites →https://doi.org/10.1021/bi971066iopenalex-snapshot
Probing the Catalytic Mechanism of Sulfite Reductase by X-ray Crystallography: Structures of the Escherichia coli Hemoprotein in Complex with Substrates, Inhibitors, Intermediates, and Products,
inferredcites →https://doi.org/10.1021/ja00076a003openalex-snapshot
Enzymic reduction of inorganic anions. Pre-steady-state kinetic analysis of the dissimilatory sulfite reductase (desulfoviridin) from Desulfovibrio vulgaris (Hildenborough). Mechanistic implications
inferredcites →https://doi.org/10.1021/ja00212a013openalex-snapshot
Characterization of two dissimilatory sulfite reductases (desulforubidin and desulfoviridin) from the sulfate-reducing bacteria. Moessbauer and EPR studies
inferredcites →https://doi.org/10.1021/ja0206487openalex-snapshot
Mechanism of the Six-Electron Reduction of Nitrite to Ammonia by CytochromecNitrite Reductase
inferredcites →https://doi.org/10.1038/37052openalex-snapshot
The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus
inferredcites →https://doi.org/10.1046/j.0014-2956.2001.02529.xopenalex-snapshot
Solution structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase
inferredcites →https://doi.org/10.1074/jbc.m502560200openalex-snapshot
Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis Is a Sulfite Reductase with a Covalent Cys-Tyr Bond in the Active Site
inferredcites →https://doi.org/10.1074/jbc.m805643200openalex-snapshot
The Crystal Structure of Desulfovibrio vulgaris Dissimilatory Sulfite Reductase Bound to DsrC Provides Novel Insights into the Mechanism of Sulfate Respiration
inferredcites →https://doi.org/10.1089/ast.2005.5.18openalex-snapshot
Domain Evolution and Functional Diversification of Sulfite Reductases
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a128985openalex-snapshot
Intermediary Formation of Trithionate in Sulfite Reduction by a Sulfate-Reducing Bacterium
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a130420openalex-snapshot
Biochemical Studies on Sulfate-reducing Bacteria
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a135144openalex-snapshot
Purification and Properties of Thiosulfate Reductase from Desulfovibrio vulgaris, Miyazaki F1
inferredcites →https://doi.org/10.1099/00221287-139-8-1817openalex-snapshot
Dissimilatory sulphite reductase from Archaeoglobus fulgidus: physico-chemical properties of the enzyme and cloning, sequencing and analysis of the reductase genes
inferredcites →https://doi.org/10.1107/s0021889893005588openalex-snapshot
Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
inferredcites →https://doi.org/10.1111/j.1432-1033.1992.tb16976.xopenalex-snapshot
Purification and biochemical characterization of a putative [6Fe‐6S] prismane‐cluster‐containing protein from Desulfovibrio vulgaris (Hildenborough)
inferredcites →https://doi.org/10.1111/j.1432-1033.1995.873_3.xopenalex-snapshot
Molecular Properties of the Dissimilatory Sulfite Reductase from Desulfovibrio Desulfuricans (Essex) and Comparison with the Enzyme from Desulfovibrio Vulgaris (Hildenborough)
inferredcites →https://doi.org/10.1111/j.1432-1033.1996.0724w.xopenalex-snapshot
Dissimilatory Sulfite Reductase Revisited
inferredcites →https://doi.org/10.1126/science.236.4803.822openalex-snapshot
Isolation of Extremely Thermophilic Sulfate Reducers: Evidence for a Novel Branch of Archaebacteria
inferredcites →https://doi.org/10.1126/science.270.5233.59openalex-snapshot
Sulfite Reductase Structure at 1.6 Å: Evolution and Catalysis for Reduction of Inorganic Anions
inferredcites →https://doi.org/10.1128/jb.132.1.139-143.1977openalex-snapshot
Bisulfite reductase of Desulfovibrio vulgaris: explanation for product formation
inferredcites →https://doi.org/10.1128/jb.136.3.916-923.1978openalex-snapshot
Dissimilatory reduction of bisulfite by Desulfovibrio vulgaris
inferredcites →https://doi.org/10.1128/jb.153.3.1211-1220.1983openalex-snapshot
Characterization of a New Type of Dissimilatory Sulfite Reductase Present in Thermodesulfobacterium commune
inferredcites →https://doi.org/10.1128/jb.163.2.472-475.1985openalex-snapshot
Characterization of a trithionate reductase system from Desulfovibrio vulgaris
inferredcites →https://doi.org/10.1128/jb.180.11.2975-2982.1998openalex-snapshot
Phylogeny of Dissimilatory Sulfite Reductases Supports an Early Origin of Sulfate Respiration
inferredcites →https://doi.org/10.1128/jb.183.8.2463-2475.2001openalex-snapshot
The Alternative Electron Acceptor Tetrathionate Supports B 12 -Dependent Anaerobic Growth of Salmonella enterica Serovar Typhimurium on Ethanolamine or 1,2-Propanediol
inferredcites →https://doi.org/10.1128/jb.98.2.429-433.1969openalex-snapshot
Thiosulfate Reductase Isolated from Desulfotomaculum nigrificans
inferredcites →https://doi.org/10.4319/lo.1969.14.3.0454openalex-snapshot
SPECTROPHOTOMETRIC DETERMINATION OF HYDROGEN SULFIDE IN NATURAL WATERS1
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.4678160openalex-extracted
Bio Processes Generating Micp and Identification of the Functional Bio Processes During Soil Modification
inferred← citeshttps://doi.org/10.1002/9781119129301.ch16openalex-snapshot
Heme Proteins – Structure and Function
inferred← citeshttps://doi.org/10.1002/9781119951438.eibc2487openalex-snapshot
Siroheme Assembly and Insertion into Nitrite and Sulfite Reductase
inferred← citeshttps://doi.org/10.1002/ange.202215235openalex-snapshot
Reduction of Sulfur Dioxide to Sulfur Monoxide by Ferrous Porphyrin**
inferred← citeshttps://doi.org/10.1002/anie.202215235openalex-snapshot
Reduction of Sulfur Dioxide to Sulfur Monoxide by Ferrous Porphyrin**
inferred← citeshttps://doi.org/10.1002/asia.202401806openalex-snapshot
Synthesis of Iron Porphyrin with Pendant Thiol Groups: Progress Toward a Model of the Heme/Cu Active Site of Sulfite Reductase
inferred← citeshttps://doi.org/10.1002/bab.1985openalex-snapshot
Mimochrome, a metalloporphyrin‐based catalytic Swiss knife†
inferred← citeshttps://doi.org/10.1002/cbdv.201100442openalex-snapshot
X‐Ray Crystal Structure of a Mutant Assimilatory Nitrite Reductase That Shows Sulfite Reductase‐Like Activity
inferred← citeshttps://doi.org/10.1002/chem.202104342openalex-snapshot
Cross‐talk Between (Hydrogen)Sulfite and Metalloproteins: Impact on Human Health
inferred← citeshttps://doi.org/10.1002/cphc.202400327openalex-snapshot
Reaction Mechanism Catalyzed by the Dissimilatory Sulfite Reductase – The Role of the Siroheme‐[4FeS4] Cofactor
inferred← citeshttps://doi.org/10.1002/ejic.201300308openalex-snapshot
Connecting [4Fe–4S] Clusters and Hemes – Towards Modeling the Active Site of Sulfite Reductase
inferred← citeshttps://doi.org/10.1002/ejic.202200739openalex-snapshot
Fifty Years of Inorganic Biomimetic Chemistry: From the Complexation of Single Metal Cations to Polynuclear Metal Complexes by Multidentate Thiolate Ligands
inferred← citeshttps://doi.org/10.1002/elan.201700317openalex-snapshot
Catalytic Reduction of Bisulfite by Myoglobin/Surfactant Films
inferred← citeshttps://doi.org/10.1002/pro.2025openalex-snapshot
Structure–function relationship of assimilatory nitrite reductases from the leaf and root of tobacco based on high‐resolution structures
inferred← citeshttps://doi.org/10.1002/prot.24094openalex-snapshot
The reductive reaction mechanism of tobacco nitrite reductase derived from a combination of crystal structures and ultraviolet–visible microspectroscopy
inferred← citeshttps://doi.org/10.1002/prot.26315openalex-snapshot
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inferred← citeshttps://doi.org/10.1007/978-3-030-18768-2_10openalex-snapshot
Respiratory Membrane Protein Complexes Convert Chemical Energy
inferred← citeshttps://doi.org/10.1007/978-3-030-96703-1_3openalex-snapshot
Reduction of Sulfur and Nitrogen Compounds
inferred← citeshttps://doi.org/10.1016/b978-0-12-398264-3.00001-2openalex-snapshot
Hemoproteins in Dissimilatory Sulfate- and Sulfur-Reducing Prokaryotes
inferred← citeshttps://doi.org/10.1016/b978-0-12-410515-7.00002-0openalex-snapshot
Microbial Sulfite Respiration
inferred← citeshttps://doi.org/10.1016/bs.ampbs.2015.05.002openalex-snapshot
A Post-Genomic View of the Ecophysiology, Catabolism and Biotechnological Relevance of Sulphate-Reducing Prokaryotes
inferred← citeshttps://doi.org/10.1016/j.bbabio.2014.03.007openalex-snapshot
The “bacterial heterodisulfide” DsrC is a key protein in dissimilatory sulfur metabolism
inferred← citeshttps://doi.org/10.1016/j.bbabio.2018.06.014openalex-snapshot
Expression, purification and characterization of an active C491G variant of ferredoxin sulfite reductase from Synechococcus elongatus PCC 7942
inferred← citeshttps://doi.org/10.1016/j.bbabio.2018.10.002openalex-snapshot
Significance of MccR, MccC, MccD, MccL and 8-methylmenaquinone in sulfite respiration of Wolinella succinogenes
inferred← citeshttps://doi.org/10.1016/j.bbapap.2018.05.013openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ccr.2016.10.003openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ccr.2019.01.021openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ccr.2025.216692openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.cej.2025.161759openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2022.107691openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.gca.2016.09.021openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.gca.2017.10.005openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.ica.2016.09.028openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jbc.2025.108511openalex-snapshot
In vitro sulfuration of Rhodobacter capsulatus formate dehydrogenase
inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2012.01.001openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jinorgbio.2025.113010openalex-snapshot
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inferred← citeshttps://doi.org/10.1016/j.jsb.2019.01.001openalex-snapshot
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase
inferred← citeshttps://doi.org/10.1016/j.mib.2011.03.003openalex-snapshot
Anaerobic oxidation of methane with sulfate: on the reversibility of the reactions that are catalyzed by enzymes also involved in methanogenesis from CO2
inferred← citeshttps://doi.org/10.1016/j.scitotenv.2018.03.219openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acs.biochem.8b00542openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acs.chemrev.1c01021openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/acscatal.5c00170openalex-snapshot
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inferred← citeshttps://doi.org/10.1021/jacs.3c07248openalex-snapshot
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inferred← citeshttps://doi.org/10.1038/s41467-025-58037-5openalex-snapshot
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inferred← citeshttps://doi.org/10.1038/s41589-022-01232-yopenalex-snapshot
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inferred← citeshttps://doi.org/10.1038/s41598-023-31802-6openalex-snapshot
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inferred← citeshttps://doi.org/10.1039/9781839161841-00023openalex-snapshot
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inferred← citeshttps://doi.org/10.1039/c2mt20225eopenalex-snapshot
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inferred← citeshttps://doi.org/10.1039/c3dt51714dopenalex-snapshot
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inferred← citeshttps://doi.org/10.1073/pnas.1407502111openalex-snapshot
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inferred← citeshttps://doi.org/10.1080/07391102.2026.2729819openalex-snapshot
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inferred← citeshttps://doi.org/10.1080/09593330.2018.1426640openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/femsec/fiab005openalex-snapshot
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inferred← citeshttps://doi.org/10.1093/ismejo/wrae167openalex-snapshot
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inferred← citeshttps://doi.org/10.1099/acmi.0.000482.v3openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/2022.04.07.487323openalex-snapshot
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inferred← citeshttps://doi.org/10.1101/2024.06.14.599029openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/imr.12579openalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1365-2958.2011.07906.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1462-2920.2012.02783.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1111/j.1472-4669.2011.00292.xopenalex-snapshot
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inferred← citeshttps://doi.org/10.1128/jb.00078-22openalex-snapshot
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inferred← citeshttps://doi.org/10.1371/journal.pone.0045313openalex-snapshot
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inferred← citeshttps://doi.org/10.21203/rs.3.rs-4758050/v1openalex-snapshot
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inferred← citeshttps://doi.org/10.22159/ajpcr.2018.v11i7.26695openalex-snapshot
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inferred← citeshttps://doi.org/10.32469/10355/45734openalex-snapshot
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inferred← citeshttps://doi.org/10.33263/briac95.255271openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/fmicb.2011.00071openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/fmicb.2014.00095openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/fmicb.2014.00577openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/fmicb.2014.00591openalex-snapshot
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inferred← citeshttps://doi.org/10.3389/fmicb.2015.01392openalex-snapshot
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Cycling of sulfur redox intermediates drives microbial activity in the sulfate–methane transition zone of cold methane seeps
inferred← citeshttps://doi.org/10.70675/29ee97cazc28ez4a34za28ez577d2b8ecbfbopenalex-snapshot
Adaptation à la pression hydrostatique chez les bactéries sulfato-réductrices piézophiles du genre Desulfovibrio
inferred← citeshttps://doi.org/10.70675/3c25f69bz194bz4e74z9ae2z55ab48f97694openalex-snapshot
Spéciation et isotopie du soufre inorganique en milieu aqueux
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