{"doi":"10.1099/mic.0.022756-0","title":"Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum","abstract":"<jats:p>An unusual non-haem diiron protein, reverse rubrerythrin (revRbr), is known to be massively upregulated in response to oxidative stress in the strictly anaerobic bacterium <jats:italic>Clostridium acetobutylicum</jats:italic>. In the present study both <jats:italic>in vivo</jats:italic> and <jats:italic>in vitro</jats:italic> results demonstrate an H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> and O<jats:sub>2</jats:sub> detoxification pathway in <jats:italic>C. acetobutylicum</jats:italic> involving revRbr, rubredoxin (Rd) and NADH : rubredoxin oxidoreductase (NROR). RevRbr exhibited both NADH peroxidase (NADH : H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> oxidoreductase) and NADH oxidase (NADH : O<jats:sub>2</jats:sub> oxidoreductase) activities in <jats:italic>in vitro</jats:italic> assays using NROR as the electron-transfer intermediary from NADH to revRbr. Rd increased the NADH consumption rate by serving as an intermediary electron-transfer shuttle between NROR and revRbr. While H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> was found to be the preferred substrate for revRbr, its relative oxidase activity was found to be significantly higher than that reported for other Rbrs. A revRbr-overexpressing strain of <jats:italic>C. acetobutylicum</jats:italic> showed significantly increased tolerance to H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> and O<jats:sub>2</jats:sub> exposure. RevRbr thus appears to protect <jats:italic>C. acetobutylicum</jats:italic> against oxidative stress by functioning as the terminal component of an NADH peroxidase and NADH oxidase.</jats:p>","journal":"Microbiology","year":2009,"id":621216,"datarank":0.6862066467755076,"base_score":4.574710978503383,"endowment":4.574710978503383,"self_citation_contribution":0.6862066467755076,"citation_network_contribution":0.0,"self_endowment_contribution":0.6862066467755076,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":96,"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":1603969,"name":"Ralf-Jörg Fischer","orcid":null,"position":1,"is_corresponding":false},{"id":1603971,"name":"David A. Wampler","orcid":null,"position":2,"is_corresponding":false},{"id":535448,"name":"Donald M. Kurtz","orcid":"0000-0003-1179-1875","position":3,"is_corresponding":false},{"id":1603972,"name":"Hubert Bahl","orcid":null,"position":4,"is_corresponding":false},{"id":1603968,"name":"Oliver Riebe","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Pathway for H2O2 and O2 detoxification in Clostridium acetobutylicum","abstract":"<jats:p>An unusual non-haem diiron protein, reverse rubrerythrin (revRbr), is known to be massively upregulated in response to oxidative stress in the strictly anaerobic bacterium <jats:italic>Clostridium acetobutylicum</jats:italic>. In the present study both <jats:italic>in vivo</jats:italic> and <jats:italic>in vitro</jats:italic> results demonstrate an H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> and O<jats:sub>2</jats:sub> detoxification pathway in <jats:italic>C. acetobutylicum</jats:italic> involving revRbr, rubredoxin (Rd) and NADH : rubredoxin oxidoreductase (NROR). RevRbr exhibited both NADH peroxidase (NADH : H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> oxidoreductase) and NADH oxidase (NADH : O<jats:sub>2</jats:sub> oxidoreductase) activities in <jats:italic>in vitro</jats:italic> assays using NROR as the electron-transfer intermediary from NADH to revRbr. Rd increased the NADH consumption rate by serving as an intermediary electron-transfer shuttle between NROR and revRbr. While H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> was found to be the preferred substrate for revRbr, its relative oxidase activity was found to be significantly higher than that reported for other Rbrs. A revRbr-overexpressing strain of <jats:italic>C. acetobutylicum</jats:italic> showed significantly increased tolerance to H<jats:sub>2</jats:sub>O<jats:sub>2</jats:sub> and O<jats:sub>2</jats:sub> exposure. RevRbr thus appears to protect <jats:italic>C. acetobutylicum</jats:italic> against oxidative stress by functioning as the terminal component of an NADH peroxidase and NADH oxidase.</jats:p>","is_dataset_classified":null,"base_score":4.574710978503383,"endowment":4.574710978503383,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"19118342","pmcid":"PMC2720019","openalex_id":"https://openalex.org/W2127137800","authors":[],"funders":[{"funder_name":"NIGMS NIH HHS","grant_id":"GM040388","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM040388","title":null}],"total_grants":2,"fwci":2.4085,"citation_percentile":0.88106171,"influential_citations":0,"citation_trend":[{"year":2012,"count":4},{"year":2013,"count":5},{"year":2014,"count":5},{"year":2015,"count":8},{"year":2016,"count":5},{"year":2017,"count":4},{"year":2018,"count":6},{"year":2019,"count":9},{"year":2020,"count":6},{"year":2021,"count":7},{"year":2022,"count":2},{"year":2023,"count":4},{"year":2024,"count":2},{"year":2025,"count":10}],"oa_status":"green","license":null,"oa_locations":[{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2720019","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/2720019","host_type":"repository"},{"url":"https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.022756-0?crawler=true","host_type":"publisher"},{"url":"https://doi.org/10.1099/mic.0.022756-0","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/19118342","host_type":"repository"}],"fields_of_study":["Hemoglobin structure and function","Heme Oxygenase-1 and Carbon Monoxide","Porphyrin Metabolism and Disorders","Bacterial Proteins","Clostridium acetobutylicum","Culture Media","Gene Expression Regulation, Bacterial","Hemerythrin","Hydrogen Peroxide","Multienzyme Complexes","NADH, NADPH Oxidoreductases","Oxidative Stress","Oxygen","Peroxidases","Rubredoxins"],"mesh_terms":["Bacterial Proteins","Culture Media","Hemerythrin","Hydrogen Peroxide","Multienzyme Complexes","NADH, NADPH Oxidoreductases","Oxygen","Peroxidases","Rubredoxins","Gene Expression Regulation, Bacterial","Oxidative Stress","Clostridium acetobutylicum"],"keywords":["Clostridium acetobutylicum","Oxidoreductase","Rubredoxin","Peroxidase","Biochemistry","Chemistry","Oxidative stress","Enzyme","Biology","Ethanol"],"sdg_mappings":[{"sdg_number":0,"sdg_label":"Clean water and sanitation"}],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-03T13:41:10.395144Z","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":[]}