{"doi":"10.1099/mic.0.030320-0","title":"Identification of two [4Fe–4S]-cluster-containing hydro-lyases from Pyrococcus furiosus","abstract":"<jats:p>The hyperthermophilic archaeon<jats:italic>Pyrococcus furiosus</jats:italic>is a strict anaerobe. It is therefore not expected to use the oxidative tricarboxylic acid (TCA) cycle for energy transduction. Nonetheless, its genome encodes more putative TCA cycle enzymes than the closely related<jats:italic>Pyrococcus horikoshii</jats:italic>and<jats:italic>Pyrococcus abyssi</jats:italic>, including an aconitase (PF0201). Furthermore, a two-subunit fumarase (PF1755 and PF1754) is encoded on the<jats:italic>Pyr. furiosus</jats:italic>genome. In the present study, these three genes were heterologously overexpressed in<jats:italic>Escherichia coli</jats:italic>to enable characterization of the enzymes. PF1755 and PF1754 were shown to form a [4Fe–4S]-cluster-containing heterodimeric enzyme, able to catalyse the reversible hydratation of fumarate. The aconitase PF0201 also contained an Fe–S cluster, and catalysed the conversion from citrate to isocitrate. The fumarase belongs to the class of two-subunit, [4Fe–4S]-cluster-containing fumarate hydratases exemplified by MmcBC from<jats:italic>Pelotomaculum thermopropionicum</jats:italic>; the aconitase belongs to the aconitase A family. Aconitase probably plays a role in amino acid synthesis when the organism grows on carbohydrates. However, the function of the seemingly metabolically isolated fumarase in<jats:italic>Pyr. furiosus</jats:italic>has yet to be established.</jats:p>","journal":"Microbiology","year":2009,"id":677495,"datarank":0.49983067652628066,"base_score":3.332204510175204,"endowment":3.332204510175204,"self_citation_contribution":0.49983067652628066,"citation_network_contribution":0.0,"self_endowment_contribution":0.49983067652628066,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":27,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1770201,"name":"Laura van der Weel","orcid":null,"position":1,"is_corresponding":false},{"id":132034,"name":"Wilfred R. 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In the present study, these three genes were heterologously overexpressed in<jats:italic>Escherichia coli</jats:italic>to enable characterization of the enzymes. PF1755 and PF1754 were shown to form a [4Fe–4S]-cluster-containing heterodimeric enzyme, able to catalyse the reversible hydratation of fumarate. The aconitase PF0201 also contained an Fe–S cluster, and catalysed the conversion from citrate to isocitrate. The fumarase belongs to the class of two-subunit, [4Fe–4S]-cluster-containing fumarate hydratases exemplified by MmcBC from<jats:italic>Pelotomaculum thermopropionicum</jats:italic>; the aconitase belongs to the aconitase A family. Aconitase probably plays a role in amino acid synthesis when the organism grows on carbohydrates. However, the function of the seemingly metabolically isolated fumarase in<jats:italic>Pyr. furiosus</jats:italic>has yet to be established.</jats:p>","is_dataset_classified":null,"base_score":3.332204510175204,"endowment":3.332204510175204,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19520720","pmcid":null,"openalex_id":"https://openalex.org/W2138604855","authors":[],"funders":[],"total_grants":0,"fwci":0.7926,"citation_percentile":0.72477749,"influential_citations":0,"citation_trend":[{"year":2012,"count":2},{"year":2013,"count":5},{"year":2014,"count":3},{"year":2015,"count":2},{"year":2017,"count":2},{"year":2018,"count":1},{"year":2019,"count":1},{"year":2020,"count":1},{"year":2021,"count":1},{"year":2022,"count":2},{"year":2023,"count":4}],"oa_status":"closed","license":null,"oa_locations":[{"url":"https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.030320-0?crawler=true","host_type":"publisher"},{"url":"https://doi.org/10.1099/mic.0.030320-0","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/19520720","host_type":"repository"}],"fields_of_study":["Enzyme Structure and Function","Metalloenzymes and iron-sulfur proteins","Enzyme Catalysis and Immobilization","Aconitate Hydratase","Amino Acid Sequence","Bacterial Proteins","Citric Acid Cycle","Escherichia coli","Fumarate Hydratase","Iron-Sulfur Proteins","Molecular Sequence Data","Pyrococcus furiosus","Sequence Alignment","Sequence Analysis, Protein","Spectrum Analysis"],"mesh_terms":["Aconitate Hydratase","Amino Acid Sequence","Bacterial Proteins","Citric Acid Cycle","Escherichia coli","Fumarate Hydratase","Iron-Sulfur Proteins","Molecular Sequence Data","Spectrum Analysis","Sequence Alignment","Pyrococcus furiosus","Sequence Analysis, Protein"],"keywords":["Pyrococcus furiosus","Aconitase","Fumarase","Biochemistry","Citric acid cycle","Escherichia coli","Protein subunit","Gene cluster","Chemistry","Fumarate reductase","Gene","Biology","Lyase","Enzyme"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-17T04:12:17.610209Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}