{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lu Z"],"funding":["Office of Extramural Research, National Institutes of Health","NIGMS NIH HHS"],"pagination":["E3266-E3275"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5889672"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["115(14)"],"pubmed_abstract":["It has been unclear whether superoxide and/or hydrogen peroxide play important roles in the phenomenon of obligate anaerobiosis. This question was explored using <i>Bacteroides thetaiotaomicron</i>, a major fermentative bacterium in the human gastrointestinal tract. Aeration inactivated two enzyme families-[4Fe-4S] dehydratases and nonredox mononuclear iron enzymes-whose homologs, in contrast, remain active in aerobic <i>Escherichia coli</i> Inactivation-rate measurements of one such enzyme, <i>B. thetaiotaomicron</i> fumarase, showed that it is no more intrinsically sensitive to oxidants than is an <i>E. coli</i> fumarase. Indeed, when the <i>E. coli</i> enzymes were expressed in <i>B. thetaiotaomicron</i>, they no longer could tolerate aeration; conversely, the <i>B. thetaiotaomicron</i>"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Endogenous superoxide is a key effector of the oxygen sensitivity of a model obligate anaerobe."],"pmcid":["PMC5889672"],"funding_grant_id":["GM049640","R37 GM049640","R01 GM049640"],"pubmed_authors":["Imlay JA","Sethu R","Lu Z"],"additional_accession":[]},"is_claimable":false,"name":"Endogenous superoxide is a key effector of the oxygen sensitivity of a model obligate anaerobe.","description":"It has been unclear whether superoxide and/or hydrogen peroxide play important roles in the phenomenon of obligate anaerobiosis. This question was explored using <i>Bacteroides thetaiotaomicron</i>, a major fermentative bacterium in the human gastrointestinal tract. Aeration inactivated two enzyme families-[4Fe-4S] dehydratases and nonredox mononuclear iron enzymes-whose homologs, in contrast, remain active in aerobic <i>Escherichia coli</i> Inactivation-rate measurements of one such enzyme, <i>B. thetaiotaomicron</i> fumarase, showed that it is no more intrinsically sensitive to oxidants than is an <i>E. coli</i> fumarase. Indeed, when the <i>E. coli</i> enzymes were expressed in <i>B. thetaiotaomicron</i>, they no longer could tolerate aeration; conversely, the <i>B. thetaiotaomicron</i>","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Apr","modification":"2025-04-26T18:12:50.112Z","creation":"2019-03-26T23:58:08Z"},"accession":"S-EPMC5889672","cross_references":{"pubmed":["29559534"],"doi":["10.1073/pnas.1800120115"]}}