<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Lu Z</submitter><funding>Office of Extramural Research, National Institutes of Health</funding><funding>NIGMS NIH HHS</funding><pagination>E3266-E3275</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5889672</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>115(14)</volume><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 &lt;i>Bacteroides thetaiotaomicron&lt;/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 &lt;i>Escherichia coli&lt;/i> Inactivation-rate measurements of one such enzyme, &lt;i>B. thetaiotaomicron&lt;/i> fumarase, showed that it is no more intrinsically sensitive to oxidants than is an &lt;i>E. coli&lt;/i> fumarase. Indeed, when the &lt;i>E. coli&lt;/i> enzymes were expressed in &lt;i>B. thetaiotaomicron&lt;/i>, they no longer could tolerate aeration; conversely, the &lt;i>B. thetaiotaomicron&lt;/i></pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>Endogenous superoxide is a key effector of the oxygen sensitivity of a model obligate anaerobe.</pubmed_title><pmcid>PMC5889672</pmcid><funding_grant_id>GM049640</funding_grant_id><funding_grant_id>R37 GM049640</funding_grant_id><funding_grant_id>R01 GM049640</funding_grant_id><pubmed_authors>Imlay JA</pubmed_authors><pubmed_authors>Sethu R</pubmed_authors><pubmed_authors>Lu Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Endogenous superoxide is a key effector of the oxygen sensitivity of a model obligate anaerobe.</name><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 &lt;i>Bacteroides thetaiotaomicron&lt;/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 &lt;i>Escherichia coli&lt;/i> Inactivation-rate measurements of one such enzyme, &lt;i>B. thetaiotaomicron&lt;/i> fumarase, showed that it is no more intrinsically sensitive to oxidants than is an &lt;i>E. coli&lt;/i> fumarase. Indeed, when the &lt;i>E. coli&lt;/i> enzymes were expressed in &lt;i>B. thetaiotaomicron&lt;/i>, they no longer could tolerate aeration; conversely, the &lt;i>B. thetaiotaomicron&lt;/i></description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Apr</publication><modification>2025-04-26T18:12:50.112Z</modification><creation>2019-03-26T23:58:08Z</creation></dates><accession>S-EPMC5889672</accession><cross_references><pubmed>29559534</pubmed><doi>10.1073/pnas.1800120115</doi></cross_references></HashMap>