<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Mangan NM</submitter><funding>U.S. Department of Energy</funding><funding>European Research Council</funding><pagination>E5354-62</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5018799</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>113(36)</volume><pubmed_abstract>Many carbon-fixing bacteria rely on a CO2 concentrating mechanism (CCM) to elevate the CO2 concentration around the carboxylating enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO). The CCM is postulated to simultaneously enhance the rate of carboxylation and minimize oxygenation, a competitive reaction with O2 also catalyzed by RuBisCO. To achieve this effect, the CCM combines two features: active transport of inorganic carbon into the cell and colocalization of carbonic anhydrase and RuBisCO inside proteinaceous microcompartments called carboxysomes. Understanding the significance of the various CCM components requires reconciling biochemical intuition with a quantitative description of the system. To this end, we have developed a mathematical model of the CCM to analyze its en</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pubmed_title>pH determines the energetic efficiency of the cyanobacterial CO2 concentrating mechanism.</pubmed_title><pmcid>PMC5018799</pmcid><funding_grant_id>DE-SC0006394</funding_grant_id><funding_grant_id>NOVCARBFIX 646827</funding_grant_id><funding_grant_id>646827</funding_grant_id><pubmed_authors>Hood RD</pubmed_authors><pubmed_authors>Mangan NM</pubmed_authors><pubmed_authors>Savage DF</pubmed_authors><pubmed_authors>Flamholz A</pubmed_authors><pubmed_authors>Milo R</pubmed_authors></additional><is_claimable>false</is_claimable><name>pH determines the energetic efficiency of the cyanobacterial CO2 concentrating mechanism.</name><description>Many carbon-fixing bacteria rely on a CO2 concentrating mechanism (CCM) to elevate the CO2 concentration around the carboxylating enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO). The CCM is postulated to simultaneously enhance the rate of carboxylation and minimize oxygenation, a competitive reaction with O2 also catalyzed by RuBisCO. To achieve this effect, the CCM combines two features: active transport of inorganic carbon into the cell and colocalization of carbonic anhydrase and RuBisCO inside proteinaceous microcompartments called carboxysomes. Understanding the significance of the various CCM components requires reconciling biochemical intuition with a quantitative description of the system. To this end, we have developed a mathematical model of the CCM to analyze its en</description><dates><release>2016-01-01T00:00:00Z</release><publication>2016 Sep</publication><modification>2026-05-05T17:29:44.994Z</modification><creation>2019-03-27T02:23:56Z</creation></dates><accession>S-EPMC5018799</accession><cross_references><pubmed>27551079</pubmed><doi>10.1073/pnas.1525145113</doi></cross_references></HashMap>